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2010 | OriginalPaper | Buchkapitel

47. Protein Crystal Growth Methods

verfasst von : Andrea E. Gutiérrez-Quezada, Roberto Arreguín-Espinosa, Abel Moreno

Erschienen in: Springer Handbook of Crystal Growth

Verlag: Springer Berlin Heidelberg

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Abstract

Nowadays, advances in genomics as well as in proteomics have produced thousands of new biological macromolecules for study in structural biology, biomedicine research, and drug design projects.

Novel and classical methods of protein crystallization as well as modern techniques for two-dimensional (2-D) and three-dimensional (3-D) characterization of different biomolecules are reviewed in this chapter. Production of high-quality single crystals will be analyzed in detail from classical approaches to modern, high-throughput crystal growth methods for x-ray diffraction, as will new strategies for reducing the amount of raw materials used, accelerating the work, and increasing success rates. It will be pointed out that this work on crystallization as well as characterization is multidisciplinary. These scientific efforts are also interrelated and require close collaboration between biochemists, biophysicists, microbiologists, and molecular biologists, as well as physicists and engineers to develop new strategies and equipment for structural purposes. Finally, some of the problems faced and plans for solving them by using x-ray diffraction, neutron diffraction, and electron microscopy will be revised.

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Vorheriges Kapitel Defect Characterization in Semiconductors with Positron Annihilation Spectroscopy

Nächstes Kapitel Crystallization from Gels

47.1.

A. McPherson: Macromolecular crystallization in the structural genomics era, J. Struct. Biol. 142, 1–2 (2003)CrossRef

47.2.

D. Roses: Genome-based pharmacogenetics and the pharmaceutical industry, Nat. Rev. Drug Discov. 1, 541–549 (2002)CrossRef

47.3.

P. Kuhn, K. Wilson, M.G. Patch, R.C. Stevens: The genesis of high-throughput structure-based drug discovery using protein crystallography, Curr. Opin. Chem. Biol. 6, 704–710 (2002)CrossRef

47.4.

J.L. DeLucas, T.L. Bray, L. Nagy, K. McCombs, N. Chernov, D. Hamrick, L. Cosenza, A. Belgovskiy, B. Stoops, A. Chait: Efficient protein crystallization, J. Struct. Biol. 142, 188–206 (2003)CrossRef

47.5.

R.J. Davey: The role of the solvent in crystal growth from solution, J. Cryst. Growth 76, 637–644 (1986)ADSCrossRef

47.6.

A.G.W. Wilson: Predicting protein crystallization from a dilute solution property, Acta Crystallogr. D 50, 361–365 (1994)CrossRef

47.7.

V. Mikol, E. Hirsch, R. Giegé: Diagnostic of precipitant for biomacromolecule crystallization by quasi-elastic light-scattering, J. Mol. Biol. 213, 187–195 (1990)CrossRef

47.8.

W.W. Wilson: Light scattering as a diagnostic for protein crystal growth – A practical approach, J. Struct. Biol. 142, 56–65 (2003)CrossRef

47.9.

C.N. Nanev: Protein crystal nucleation, Cryst. Res. Technol. 42, 4–12 (2007)

47.10.

A.A. Chernov: Modern Crystallography III, Crystal Growth (Springer, Berlin Heidelberg 1984)CrossRef

47.11.

S. Sarig: Handbook of Crystal Growth, Vol. 2B, ed. by D.T.J. Hurle (North-Holland, Amsterdam 1994)

47.12.

P. Bennema: Crystal growth from solution – Theory and experiment, J. Cryst. Growth 24, 76–83 (1974)ADSCrossRef

47.13.

D.T.J. Hurle: Handbook of Crystal Growth, Vol. 1B (North-Holland, Amsterdam 1994)

47.14.

D.T.J. Hurle: Handbook of Crystal Growth, Vol. 2A (North-Holland, Amsterdam 1994)

47.15.

F.E. Neumann: Über die optischen Eigenschaften der hemiprismatischen oder zwei- und eingliedrigen Krystalle, Ann. Physik 111, 81–95 (1835), in GermanADSCrossRef

47.16.

F. Rosenberger: Inorganic and protein crystal growth – Similarities and differences, J. Cryst. Growth 76, 618–636 (1986)ADSCrossRef

47.17.

P.S. Cheng, P.J. Shlichta, W.R. Wilcox, R.A. Lefever: Convection phenomena during the growth of sodium chlorate crystals from solution, J. Cryst. Growth, 47, 43–60 (1979)ADSCrossRef

47.18.

A. McPherson: Macromolecular crystal growth in microgravity, Crystallogr. Rev. 6, 157–308 (1996)CrossRef

47.19.

F. Rosenberger: Fundamentals of Crystal Growth I, Macroscopic Equilibrium Concepts (Springer, Berlin Heidelberg 1979)CrossRef

47.20.

T.M. Bergfors: Protein crystallization (Int. Univ. Line, La Jolla 1999)

47.21.

A. Ducruix, R. Giegé: Crystallization of Nucleic Acids and Proteins, a Practical Approach, 2nd edn. (IRL, Oxford 1999)

47.22.

A. McPherson: Crystallization of Biological Macromolecules (Cold Spring Harbor Laboratory, New York 1999)

47.23.

R. Giegé, A. McPherson: General methods. In: International Tables for Crystallography, Vol. F, ed. by M.G. Rossmann, E. Arnold (IUCr, Kluwer Academic, Boston 2001)

47.24.

A. DʼArcy, C. Elmore, M. Stihle, J.E. Johnston: A novel approach to crystallising proteins under oil, J. Cryst. Growth 168, 175–180 (1992)CrossRef

47.25.

E.P.K. Hade, C. Tanford: Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins in concentrated aqueous cesium chloride and guanidine hydrochloride, J. Am. Chem. Soc. 89, 5034–5040 (1967)CrossRef

47.26.

J.R. Luft, J. Wolfley, I. Jurisica, J. Lasgow, S. Fortier, G.T. DeTitta: Macromolecular crystallization in a high throughput laboratory – The search phase, J. Cryst. Growth 232, 591–595 (2001)ADSCrossRef

47.27.

A. McPherson, J. Geller, A. Rich: Crystallographic studies on concanavalin B, Biochem. Biophys. Res. Commun. 57, 494–499 (1974)CrossRef

47.28.

B.H. Weber, P.E. Goodkin: A modified microdiffusion procedure for the growth of single protein crystals by concentration-gradient equilibrium dialysis, Arch. Biochem. Biophys. 141, 489–498 (1970)CrossRef

47.29.

F.R. Salemme: A free interface diffusion technique for the crystallization of proteins for X-ray crystallography, Arch. Biochem. Biophys. 151, 533–539 (1972)CrossRef

47.30.

B. Lorber, R. Giegé: Nucleation and growth of thaumatin crystals within a gel under microgravity on STS-95 mission vs. under Earthʼs gravity, J. Cryst. Growth 231, 252–261 (2001)ADSCrossRef

47.31.

M. Ataka, E. Katoh, N.I. Wakayama: Magnetic orientation as a tool to study the initial stage of crystallization of lysozyme, J. Cryst. Growth 173, 592–596 (1997)ADSCrossRef

47.32.

N.I. Wakayama, M. Ataka, H. Abe: Effect of a magnetic field gradient on the crystallization of hen lysozyme, J. Cryst. Growth 178, 653–656 (1997)ADSCrossRef

47.33.

J.M.. García-Ruíz, M.L. Novella, R. Moreno, J.A. Gavira: Agarose as crystallization media for proteins. I: Transport processes, J. Cryst. Growth 232, 165–172 (2001)ADSCrossRef

47.34.

M. Pusey, W.K. Witherow, R. Naumann: Preliminary investigations into solutal flow about growing tetragonal lysozyme crystals, J. Cryst. Growth 90, 105–111 (1988)ADSCrossRef

47.35.

M. Beth, H. Broom, W.K. Witherow, R.S. Snyder, D.C. Carter: Preliminary observations of the effect of solutal convection on crystal morphology, J. Cryst. Growth, 90, 130–135 (1988)ADSCrossRef

47.36.

J.K. Baird, E.J. Meehan, A.L. Xidis, S.B. Howard: Convective diffusion in protein crystal growth, J. Cryst. Growth 76, 694–700 (1986)ADSCrossRef

47.37.

H. Lin, F. Rosenberger, J.L.D. Alexander, A. Nadarajah: Convective-diffusive transport in protein crystal growth, J. Cryst. Growth 151, 153–162 (1995)ADSCrossRef

47.38.

Y.P. Wang, Y. Han, J.S. Pan, K.Y. Wang, R.C. Bi: Protein crystal growth in microgravity using a liquid/liquid diffusion method, Microgravity Sci. Technol. 9, 281–283 (1996)

47.39.

W. Littke, C. John: Protein single crystal growth under microgravity, Science 225, 203–204 (1984)ADSCrossRef

47.40.

A. McPherson: Methods of Biochemical Analysis, Vol. 23, ed. by D. Glick (Academic, New York 1976)

47.41.

A. McPherson: The Preparation and Analysis of Protein Crystals (Wiley, New York 1982)

47.42.

J.L. DeLucas, C.D. Smith, H.W. Smith, V.K. Senagdi, S.E. Senadhi, S.E. Ealick, C.E. Bugg, D.C. Carter, R.S. Snyder, P.C. Weber, F.R. Salemme, D.H. Ohlendorf, H.M. Einspahr, L. Clancy, M.A. Navia, B. McKeever, T.L. Nagabhushan, G. Nelson, Y.S. Babu, A. McPherson, S. Koszelak, D. Stammers, K. Powell, G. Darby: Protein crystal growth in microgravity, Science 246, 651–654 (1989)ADSCrossRef

47.43.

R.S. Snyder, K. Fuhrmann, H.U. Walter: Protein crystallization facilities for microgravity experiments, J. Cryst. Growth 110, 333–338 (1991)ADSCrossRef

47.44.

M.M. Long, L.J. DeLucas, C. Smith, M. Carson, K. Moore, M.D. Harrington, D.J. Pilion, S.P. Bishop, W.M. Rosenblum, R.J. Naumann, A. Chait, J. Prahl, C.E. Bugg: Protein crystals growth in microgravity–temperature induced large scale crystallization of insulin, Microgravity Sci. Technol. 7, 196–202 (1994)

47.45.

J.L. DeLucas, F.L. Suddath, R. Snyder, R. Naumann, M.B. Broom, M. Pusey, V. Yost, B. Herren, D. Carter, B. Nelson, E.J. Meehan, A. McPherson, C.E. Bugg: Preliminary investigations of protein crystal growth using the space shuttle, J. Cryst. Growth 76, 681–693 (1986)ADSCrossRef

47.46.

J.L. DeLucas, M.M. Long, K.M. Moore, W.M. Rosenblum, T.L. Bray, C. Smith, M. Carson, S.V.L. Narayana, D. Carter, A.D. Clark Jr., R.G. Nanni, J. Ding, A. Jacobo-Molina, G. Kamer, S.H. Hughes, E. Arnold, H.M. Einspahr, L.L. Clancy, G.S.J. Rao, P.F. Cook, B.G. Harris, S.H. Munson, B.C. Finzel, A. McPherson, P.C. Weber, F. Lewandowski, T.L. Nagabhushan, P.P. Trotta, P. Reichert, M.A. Navia, K.P. Wilson, J.A. Thomson, R.R. Richards, K.D. Bowersox, C.J. Meade, E.S. Baker, S.P. Bishop, B.J. Dunbar, E. Trinh, J. Prahl, A. Sacco Jr., C.E. Bugg: Recent results and new hardware developments for protein crystal growth in microgravity, J. Cryst. Growth 135, 183–195 (1994)ADSCrossRef

47.47.

J.R. Helliwell, E. Snell, S. Weisgerber: Proc. 9th Europ. Symp. Gravity Depend. Phenom. Phys. Sci. (Berlin 1995)

47.48.

E.H. Snell, S. Weisgerber, J.R. Helliwell: Improvements in lysozyme protein crystal perfection through microgravity growth, Acta Crystallogr. D 51, 1099–1102 (1995)CrossRef

47.49.

R. Boistelle, J.P. Astier: Crystallization mechanisms in solution, J. Cryst. Growth, 90, 14–30 (1988)ADSCrossRef

47.50.

H.K. Henisch: Crystals in Gels and Liesegang Rings (Cambridge Univ. Press, Cambridge 1988)CrossRef

47.51.

K.-T. Wilke: Kristallzüchtung (Verlag Harri Deutsch, Frankfurt/Main 1988), in German

47.52.

P.S. Chen, P.J. Schlichta, W.R. Wilcox, R.A. Lefever: Convection phenomena during the growth of sodium chlorate crystals from solution, J. Cryst. Growth 47, 43–60 (1979)ADSCrossRef

47.53.

M.C. Robert, F. Lefaucheux: Crystal growth in gels: Principle and applications, J. Cryst. Growth 90, 358–367 (1988)ADSCrossRef

47.54.

B. Rubin: The growth of single crystals by controlled diffusion in silica gel, AIChe J. 15, 206–208 (1969)CrossRef

47.55.

M.C. Robert, F. Lefaucheux, B. Jannot, G. Godefroy, E. Garnier: A comparative study of gel grown and space grown lead hydrogen phosphate crystals, J. Cryst. Growth 88, 499–510 (1988)ADSCrossRef

47.56.

J.M. García-Ruiz, O. Fermín, M.L. Novella, J.A. Gavira, C. Sauter, O. Vidal: A supersaturation wave of protein crystallization, J. Cryst. Growth 232, 149–155 (2001)ADSCrossRef

47.57.

B.W. Low, F.M. Richards: Measurements of the density, composition and related unit cell dimensions of some protein crystals, J. Am. Chem. Soc. 76, 2511–2518 (1954)CrossRef

47.58.

B. Lorber, C. Sauter, M.C. Robert, B. Capelle, R. Giegé: Crystallization within agarose gel in microgravity improves the quality of thaumatin crystals, Acta Crystallogr. D 55, 1491–1494 (1999)CrossRef

47.59.

D. Maes, L.A. Gonzalez-Ramirez, J. Lopez-Jaramillo, B. Yu, H. De Bondt, I. Zegers, E. Afonina, J.M. García-Ruiz, S. Gulnik: Structural study of the type II 3-dehydroquinate dehydratase from Actinobacillus pleuropneumoniae, Acta Crystallogr. D 60, 463–471 (2004)CrossRef

47.60.

J.M. García-Ruiz: Counterdiffusion methods for macromolecular crystallization, Methods Enzymol. 368, 130–154 (2003)CrossRef

47.61.

F. Otálora, J.M. García-Ruiz, A. Moreno: Protein crystal quality studies using rod-shaped crystals, J. Cryst. Growth 168, 93–98 (1996)ADSCrossRef

47.62.

A. McPherson, A.J. Makin, Y.G. Kuznetsov, S. Koszelak, M. Wells, G. Jenkins, G. Howard, J. Lawson: The effects of microgravity on protein crystallization: evidence for concentration gradients around growing crystals, J. Cryst. Growth 196, 572–586 (1988)ADSCrossRef

47.63.

F. Otálora, J.M. García-Ruiz, L. Carotenuto, D. Castagnolo, M.L. Novella, A.A. Chernov: Lysozyme crystal growth kinetics in microgravity, Acta Crystallogr. D 58, 1681–1689 (2002)CrossRef

47.64.

M. Zeppezauer, H. Eklund, E.S. Zeppezauer: Micro diffusion cells for the growth of single protein crystals by means of equilibrium dialysis, Arch. Biochem. Biophys. 126, 564–573 (1968)CrossRef

47.65.

A. Yonath, J. Müssig, H.G. Witlmann: Parameters for crystal growth of ribosomal subunits, J. Cell. Biochem. 19, 145–155 (1982)CrossRef

47.66.

J.M. García-Ruíz: The uses of crystal growth in gels and other diffusing-reacting systems, Key Eng. Mater. 58, 87–106 (1991)CrossRef

47.67.

J.M. García-Ruíz, A. Moreno, C. Viedma, M. Coll: Crystal quality of lysozyme single crystals grown by the gel acupuncture method, Mater. Res. Bull. 28, 541–546 (1993)CrossRef

47.68.

J.M. García-Ruíz, A. Moreno: Investigations on protein crystal growth by the gel acupuncture method, Acta Crystallogr. D 50, 484–490 (1994)CrossRef

47.69.

V.M. Bolaños-García: The use of oil in a counter-diffusive system allows to control nucleation and coarsening during protein crystallization, J. Cryst. Growth 253, 517–523 (2003)ADSCrossRef

47.70.

J.M. García-Ruíz, A. Moreno, D. Rondón, F. Otálora, F. Zauscher: Teaching protein crystallization by the gel acupuncture technique, J. Chem. Educ. 75, 442–446 (1998)CrossRef

47.71.

J.D. Ng, J.A. Gavira, J.M. García-Ruíz: Protein crystallization by capillary counterdiffusion for applied crystallographic structure determination, J. Struct. Biol. 142, 218–231 (2003)CrossRef

47.72.

J.A. Gavira, D. Toh, J. Lopez-Jaramillo, J.M. García-Ruíz, J.D. Ng: Ab initio crystallographic structure determination of insulin from protein to electron density without crystal handling, Acta Crystallogr. D 58, 1147–1154 (2002)CrossRef

47.73.

C. Biertümpfel, J. Basquin, D. Suck, C. Sauter: Crystallization of biological macromolecules using agarose gel, Acta Crystallogr. D 58, 1657–1659 (2002)CrossRef

47.74.

N. Mirkin, B.A. Frontana-Uribe, A. Rodriguez-Romero, A. Hernandez-Santoyo, A. Moreno: The influence of an internal electric field upon protein crystallization using the gel-acupuncture method, Acta Crystallogr. D 59, 1533–1538 (2003)CrossRef

47.75.

M. Taleb, C. Didierjean, C. Jelsch, J.P. Mangeot, A. Aubry: Equilibrium kinetics of lysozyme crystallization under an external electric field, J. Cryst. Growth 232, 250–255 (2001)ADSCrossRef

47.76.

C. Nanev, A. Penkova: Nucleation of lysozyme crystals under external electric and ultrasonic fields, J. Cryst. Growth 232, 285–293 (2001)ADSCrossRef

47.77.

M.I. Al-Haq, E. Lebrasseur, H. Tsuchiya, T. Torii: Protein crystallization under an electric field, Crystallogr. Rev. 13, 29–64 (2007)CrossRef

47.78.

E. Nieto-Mendoza, B. Frontana-Uribe, G. Sazaki, A. Moreno: Investigations on electromigration phenomena for protein crystallization using crystal growth cells with multiple electrodes, effect of the potential control, J. Cryst. Growth 275, 1443–1452 (2005)CrossRef

47.79.

A. Moreno, G. Sazaki: The use of a new ad hoc growth cell with parallel electrodes for the nucleation control of lysozyme, J. Cryst. Growth 264, 438–444 (2004)ADSCrossRef

47.80.

G. Sazaki, A. Moreno, K. Nakajima: Novel coupling effects of the magnetic and electric fields on protein crystallization, J. Cryst. Growth 262, 499–502 (2004)ADSCrossRef

47.81.

A. Penkova, O. Gliko, I.L.D. Feyzim, V. Hodjaoglu, C. Nanev, P.G. Vekilov: Enhancement and suppression of protein crystal nucleation due to electrically driven convection, J. Cryst. Growth 275, e1527–e1532 (2005)ADSCrossRef

47.82.

G. Sazaki, E. Yoshida, H. Komatsu, T. Nakada, S. Miyashita, K. Watanabe: Effects of a magnetic field on the nucleation and growth of protein crystals, J. Cryst. Growth 173, 231–234 (1997)ADSCrossRef

47.83.

Y. Suzuki, S. Miyashita, G. Sazaki, T. Nakada, T. Sawada, H. Komatsu: Effects of pressure on growth kinetics of tetragonal lysozyme crystals, J. Cryst. Growth 208, 638–644 (2000)ADSCrossRef

47.84.

A. Kadri, G. Jenner, M. Damak, B. Lorber, R. Giegé: Crystallogenesis studies of proteins in agarose gel–combined effect of high hydrostatic pressure and pH, J. Cryst. Growth 257, 390–402 (2003)ADSCrossRef

47.85.

Y. Mori, K. Takano, H. Adachi, T. Inoue, S. Murakami, H. Matsumura, T. Sasaki: Protein crystallization using femto-second laser irradiation and solution-stirring, Proc. 11th Int. Conf. Cryst. Biol. Macromol. (Quebec City 2006)

47.86.

A. McPherson, P. Shlichta: The use of heterogeneous and epitaxial nucleants to promote growth of protein crystals, J. Cryst. Growth 90, 47–50 (1988)ADSCrossRef

47.87.

T.E. Paxton, A. Sambanis, R.W. Rousseau: Mineral substrates as heterogeneous nucleants in the crystallization of proteins, J. Cryst. Growth 198/199, 656–660 (1999)ADSCrossRef

47.88.

N.E. Chayen, E. Saridakis, R. El-Bahar, Y. Nemirovsky: Porous silicon: An effective nucleation-inducing material for protein crystallization, J. Mol. Biol. 312, 591–595 (2001)CrossRef

47.89.

N.E. Chayen, L. Hench: (Imperial College Innovations Limited, UK) Mesoporous glass as nucleant for macromolecule crystallisation, Patent No. WO2004041847 (2003)

47.90.

R.P. Sear: Protein crystals and charged surfaces: Interactions and heterogeneous nucleation, Phys. Rev. E 67, 061907/1–061907/7 (2003)

47.91.

N.E. Chayen, E. Saridakis, R.P. Sear: Experiment and theory for heterogeneous nucleation of protein crystals in a porous medium, Proc. Natl. Acad. Sci. USA 103, 597–601 (2006)ADSCrossRef

47.92.

W.W. Wilson: Monitoring crystallization experiments using dynamic light scattering: Assaying and monitoring protein crystallization in solution, Methods Companion Methods Enzymol. 1, 110–117 (1990)CrossRef

47.93.

G. Juárez-Martínez, C. Garza, R. Castillo, A. Moreno: A dynamic light scattering investigation of the nucleation and growth of thaumatin crystals, J. Cryst. Growth 232, 119–131 (2001)ADSCrossRef

47.94.

N. Chayen, M. Dieckmann, K. Dierks, P. Fromme: Size and shape determination of proteins in solution by a noninvasive depolarized dynamic light scattering instrument, Ann N. Y. Acad. Sci. (Transport Phenomena in Microgravity), 1027, 20–27 (2004)CrossRef

47.95.

C. Chin, J.B. Dence, J.C. Warren: Crystallization of human placental estradiol 17β-dehydrogenase. A new method for crystallizing labile enzymes, J. Biol. Chem. 251, 3700–3705 (1976)

47.96.

M.C. Vaney, I. Broutin, P. Retailleau, A. Douangmath, S. Lafont, C. Hamiaux, T. Prangé, A. Ducruix, M. Riès-Kautt: Structural effects of monovalent anions on polymorphic lysozyme crystals, Acta Crystallogr. D 57, 929–940 (2001)CrossRef

47.97.

A. McPherson, J. Weickmann: X-ray analysis of new crystal forms of the sweet protein thaumatin, J. Biomol. Struct. Dyn. 7, 1053–1060 (1990)CrossRef

47.98.

J. Qi, N.I. Wakayama, M. Ataka: Magnetic suppression of convection in protein crystal growth processes, J. Cryst. Growth 232, 132–137 (2001)ADSCrossRef

47.99.

S.X. Lin, M. Zhou, A. Azzi, G.J. Xu, N.I. Wakayama, M. Ataka: Magnet used for protein crystallization: novel attempts to improve the crystal quality, Biophys. Res. Commun. 275, 274–278 (2000)CrossRef

47.100.

T. Sato, Y. Yamada, S. Saijo, T. Hori, R. Hirose, N. Tanaka, G. Sazaki, K. Nakajima, N. Igarashi, M. Tanaka, Y. Matsuura: Enhancement in the perfection of orthorhombic lysozyme crystals grown in a high magnetic field (10 T), Acta Crystallogr. D 56, 1079–1083 (2000)CrossRef

47.101.

C.W. Zhong, N.I. Wakayama: Effect of a high magnetic field on the viscosity of an aqueous solution of protein, J. Cryst. Growth 226, 327–332 (2001)ADSCrossRef

47.102.

L. Wang, C.W. Zhong, N.I. Wakayama: Damping of natural convection in the aqueous protein solutions by the application of high magnetic fields, J. Cryst. Growth 237, 312–316 (2002)ADSCrossRef

47.103.

D.C. Yin, N.I. Wakayama, Y. Inatomi, W.D. Huang, K. Kuribayashi: Strong magnetic field effect on the dissolution process of tetragonal lysozyme crystals, Adv. Space Res. 32, 217–223 (2003)ADSCrossRef

47.104.

D. Lübbert, A. Meents, E. Weckert: Accurate rocking-curve measurements on protein crystals grown in a homogeneous magnetic field of 2.4 T, Acta Crystallogr. D 60, 987–998 (2004)CrossRef

47.105.

A. Moreno, B. Quiroz-García, F. Yokaichiya, V. Stojanoff, P. Rudolph: Protein crystal growth in gels and stationary magnetic fields, Cryst. Res. Technol. 42, 231–236 (2007)CrossRef

47.106.

T. Sato, Y. Yamada, S. Saijo, T. Hori, R. Hirose, N. Tanaka, G. Sazaki, K. Nakajima, N. Igarashi, M. Tanaka, Y. Matsuura: Improvement in diffraction maxima in orthorhombic HEWL crystal grown under high magnetic field, J. Cryst. Growth 232, 229–236 (2001)ADSCrossRef

47.107.

T. Terwillinger: Structural genomics in America, Nat. Struct. Biol. 7, 935–939 (2000)CrossRef

47.108.

R. Hui, A. Edwards: High-throughput protein crystallization, J. Struct. Biol. 142, 154–161 (2003)CrossRef

47.109.

J.-W. de Gier, J. Luirink: Biogenesis of inner membrane proteins in Escherichia coli, J. Mol. Microbiol. 40, 314–322 (2001)CrossRef

47.110.

S.A. Lesley: High-throughput proteomics: Protein expression and purification in the postgenomic world, Protein Expr. Purif. 22, 159–164 (2001)CrossRef

47.111.

Stephen White: http://blanco.biomol.uci.edu/Membrane_Proteins_xtal.html (2009)

47.112.

R. Grisshammer, C.G. Tate: Overexpression of integral membrane proteins for structural studies, Q. Rev. Biophys. 28, 315–422 (1995)CrossRef

47.113.

A. Arora, D. Rinehart, G. Szabo, L.K. Tamm: Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers, J. Biol. Chem. 275, 1594–1600 (2000)CrossRef

47.114.

M. Müller, H.G. Koch, K. Beck, U. Schäfer: Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane, Prog. Nucleic Acid Res. Mol. Biol. 66, 107–157 (2001)CrossRef

47.115.

G. Chang, R.H. Spencer, A.T. Lee, M.T. Barclay, D.C. Rees: Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel, Science 282, 2220–2226 (1998)ADSCrossRef

47.116.

C.G. Tate: Overexpression of mammalian integral membrane proteins for structural studies, FEBS Letters 504, 94–98 (2001)CrossRef

47.117.

K.E.S. Matlack, W. Mothes, T.A. Rapoport: Protein translocation: Tunnel vision, Cell 92, 381–390 (1998)CrossRef

47.118.

J.C. Otto, D.L. De Witt, W.L. Smith: N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum, J. Biol. Chem. 268, 18234–18242 (1993)

47.119.

M.P. Patricelli, H.A. Lashuel, D.K. Giang, J.W. Kelly, B.F. Cravatt: Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: Identification of the transmembrane domain as a site for oligomerization, Biochemistry 37, 15177–15187 (1998)CrossRef

47.120.

M.H. Bracey, M.A. Hanson, K.R. Masuda, R.C. Stevens, B.F. Cravatt: Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling, Science 298, 1793–1796 (2002)ADSCrossRef

47.121.

G.J. Turner, R. Reusch, A.M. Winter-Vann, L. Martínez, M.C. Betlach: Heterologous gene expression in a membrane-protein-specific system, Protein Expr. Purif. 17, 312–323 (1999)CrossRef

47.122.

J.L. Cereghino, J.M. Cregg: Heterologous protein expression in the methylotrophic yeast Pichia pastoris, FEMS Microbiol. Rev. 24, 45–66 (2000)CrossRef

47.123.

K. Sreekrishna, R.G. Brankamp, K.E. Kropp, D.T. Blankenship, J.T. Tsay, P.L. Smith, J.D. Wierschke, A. Subramaniam, L.A. Birkenberger: Strategies for optimal synthesis and secretion of heterologous proteins in the methylotrophic yeast Pichia pastoris, Gene 190, 55–62 (1997)CrossRef

47.124.

P.J. Loll: Membrane protein structural biology: The high throughput challenge, J. Struct. Biol. 142, 144–153 (2003)CrossRef

47.125.

J.P. Rosenbusch: Stability of membrane proteins: relevance for the selection of appropriate methods for high-resolution structure determinations, J. Struct. Biol. 136, 144–157 (2001)CrossRef

47.126.

E.M. Landau, J.P. Rosenbusch: Lipidic cubic phases: A novel concept for the crystallization of membrane proteins, Proc. Natl. Acad. Sci. USA 93, 14532–14535 (1996)ADSCrossRef

47.127.

A. Cheng, B. Hummel, H. Qiu, M. Caffrey: A simple mechanical mixer for small viscous lipid-containing samples, Chem. Phys. Lipids 95, 11–21 (1998)CrossRef

47.128.

S.D. Durbin, W.E. Carlson: Lysozyme crystal growth studied by atomic force microscopy, J. Cryst. Growth 122, 71–79 (1992)ADSCrossRef

47.129.

A.J. Malkin, Y.G. Kuznetsov, A. McPherson: Incorporation of microcrystals by growing protein and virus crystals, Proteins 24, 247–252 (1996)CrossRef

47.130.

D.A. Walters, B.L. Smith, A.M. Belcher, G.T. Paloczi, G.D. Stucky, D.E. Morse, P.K. Hansma: Modification of calcite crystal growth by abalone shell proteins: an atomic force microscope study, Biophys. J. 72, 1425–1433 (1997)ADSCrossRef

47.131.

H. Li, A. Nadarajah, M.L. Pusey: Determining the molecular-growth mechanisms of protein crystal faces by atomic force microscopy, Acta Crystallogr. D 55, 1036–1045 (1999)CrossRef

47.132.

Y.F. Dufrene: Application of atomic force microscopy to microbial surfaces: From reconstituted cell surface layers to living cells, Micron 32, 153–165 (2001)CrossRef

47.133.

M. Plomp, A. McPherson, A.J. Malkin: Repair of impurity-poisoned protein crystal surfaces, Proteins 50, 486–495 (2003)CrossRef

47.134.

A.J. Malkin, R.E. Thorne: Growth and disorder of macromolecular crystals: Insights from atomic force microscopy and X-ray diffraction studies, Methods 34, 273–299 (2004)CrossRef

47.135.

S. Hiroyuki: Modification, characterization and handling of protein molecules as the first step to bioelectronic devices, Electron. Biotechnol. Adv. (EL.B.A.) Forum Ser. 2, 157–174 (1996)

47.136.

I. Reviakine, W. Bergsma-Schutter, A. Brisson: Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM, J. Struct. Biol. 121, 356–361 (1998)CrossRef

47.137.

S.-T. Yau, B.R. Thomas, P.G. Vekilov: Molecular mechanisms of crystallization and defect formation, Phys. Rev. Lett. 85, 353–356 (2000)ADSCrossRef

47.138.

A.P. Wheeler, C.S. Sikes: Proteins from oyster shell: biomineralization regulators and commercial polymer analogs, Mater. Res. Soc. Symp. Proc. 599, 209–224 (2000)CrossRef

47.139.

H. Kim, R.M. Garavito, R. Lal: Atomic force microscopy of the three-dimensional crystal of membrane protein, OmpC porin, Colloids Surf. B: Biointerfaces 19, 347–355 (2000)CrossRef

47.140.

A. Nadarajah, H. Li, J.H. Konnert, M.L. Pusey: New AFM techniques for investigating molecular growth mechanisms of protein crystals, Proc. SPIE 4098, 31–39 (2000)ADSCrossRef

47.141.

A. McPherson: Macromolecular crystal structure and properties as revealed by atomic force microscopy, NATO Sci. Ser. I: Life Behav. Sci. 325, 1–8 (2001)

47.142.

A. McPherson, A.J. Malkin, Y.G. Kuznetsov: Atomic force microscopy in the study of macromolecular crystal growth, Annu. Rev. Biophys. Biomol. Struct., 29, 361–410 (2000)CrossRef

47.143.

J. Yang, L.K. Tamm, T.W. Tillack, Z. Shao: New approach for atomic-force microscopy of membrane proteins. The imaging of cholera toxin, J. Mol. Biol. 229, 286–290 (1993)CrossRef

47.144.

P. Hallett, G. Offer, M.J. Miles: Atomic force microscopy of the myosin molecule, Biophys. J. 68, 1604–1606 (1995)CrossRef

47.145.

D. Pang, S. Yoo, W.S. Dynan, M. Jung, A. Dritschilo: Ku proteins join DNA fragments as shown by atomic force microscopy, Cancer Res. 57, 1412–1415 (1997)

47.146.

K.K. Chittur: Proteins on surfaces: methodologies for surface preparation and engineering protein function, Surfact. Sci. Ser. 75, 143–179 (1998)

47.147.

J. Cao, D.K. Pham, L. Tonge, D.V. Nicolau: Simulation of the force-distance curves of atomic force microscopy for proteins by the Connolly surface approach, Proc. SPIE 4590, 187–194 (2001)ADSCrossRef

47.148.

W. Huang, S. Taylor, K. Fu, Y. Lin, D. Zhang, T.W. Hanks, A.M. Rao, Y.-P. Sun: Attaching proteins to carbon nanotubes via diimide-activated amidation, Nano Lett. 2, 311–314 (2002)ADSCrossRef

47.149.

J. Torres, T.J. Stevens, M. Samso: Membrane proteins: the "Wild West" of structural biology, Trends Biochem. Sci. 28, 137–144 (2003)CrossRef

47.150.

A. Tulpar, D.B. Henderson, M. Mao, B. Caba, R.M. Davis, K.E. Van Cott, W.A. Ducker: Unnatural proteins for the control of surface forces, Langmuir 21, 1497–1506 (2005)CrossRef

47.151.

P.L. Silva: Imaging proteins with atomic force microscopy: An overview, Curr. Protein Peptide Sci. 6, 387–395 (2005)CrossRef

47.152.

E.A. Stura, I.A. Wilson: Applications of the streak seeding technique in protein crystallization, J. Cryst. Growth 110, 270–282 (1991)ADSCrossRef

47.153.

Y. Zhang, T. Fu, H. Li, K. Xu, K. State: Co-deposition of electocrystallized calcium phosphate and protein as biocoatings on the prosthetic materials, Guisuanyan Xuebao 28, 379–380, 384 (2000), in Chinese

47.154.

A. Moreno, M. Rivera: Conceptions and first results on the electrocrystallization behaviour of ferritin, Acta Crystallogr. D 61, 1678–1681 (2005)CrossRef

47.155.

Y.H. Chen, J.Y. Wu, Y.C. Chung: Preparation of polyaniline-modified electrodes containing sulfonated polyelectrolytes using layer-by-layer techiques, Biosens. Bioelectron. 22, 489–494 (2006)CrossRef

47.156.

J.P.H. Perez, E. Lopez-Cabarcos, B. Lopez-Ruiz: The application of methacrylate-based polymers to enzyme biosensors, Biomol. Eng. 23, 233–245 (2006)CrossRef

47.157.

A. Baba, W. Knoll, R. Advincula: Simultaneous in situ electrochemical, surface plasmon optical, and atomic force microscopy measurements: Investigations of conjugated polymer electropolymerization, Rev. Sci. Instrum. 77, 064101 (2006)ADSCrossRef

47.158.

G.A. Álvarez-Romero, E. Garfias-García, M.T. Ramírez-Silva, C. Galán-Vidal, M. Romero-Romo, M. Palomar-Pardavé: Electrochemical and AFM characterization of the electropolimerization of pyrrole over a graphite–epoxy resin solid composite electrode, in the presence of different anions, Appl. Surf. Sci. 252, 5783–5792 (2006)ADSCrossRef

47.159.

T. Hernández-Pérez, N. Mirkin, A. Moreno, M. Rivera: In situ immobilization of catalase monocrystals on HOPG by the voltammetric growth of polypyrrole films for AFM investigations, Electrochem. Solid-State Lett. 5, 37–39 (2002)CrossRef

47.160.

F. Acosta, D. Eid, L. Marín-García, B.A. Frontana-Uribe, A. Moreno: From cytochrome c crystals to a solid-state electron-transfer device, Cryst. Growth. Des. 7, 2187–2191 (2008)CrossRef

47.161.

N. Mirkin, J. Jaconcic, V. Stojanoff, A. Moreno: High resolution X-ray crystallographic structure of cytochrome c from bovine heart and its application to the design of an electron transfer biosensor, Proteins: Structure, Function, Bioinformatics 70, 83–92 (2008)

47.162.

T.L. Blundell, L.N. Johnson: Protein Crystallography (Oxford Univ. Press, Oxford 1976)

47.163.

C. Giacovazzo, C. Giazovazzo, H.L. Monaco, G. Artioli, D. Viterbo, G. Ferraris: Fundamentals of Crystallography (Oxford Univ. Press, Oxford 2002)

47.164.

D.M. Blow: Outline of Crystallography for Biologists (Oxford Univ. Press, Oxford 2002)

47.165.

A. McPherson: Macromolecular Crystallography (Wiley, New York 2002)

47.166.

D.E. McRee: Practical Protein Crystallography (Academic, New York 1999)

47.167.

H.M. Einspahr: A functioning crystallization database: What do we want and how do we get it? Int. Sch. Biological Cryst. (Granada 2006)

47.168.

N. Niimura: Neutron Protein Crystallography: Hydrogen and Hydration in Proteins. Neutron Scattering in Biology (Springer, Berlin Heidelberg 2006) pp. 43–62

47.169.

D.A.A. Myles: Neutron protein crystallography: current status and brighter future, Curr. Opin. Struct. Biol. 16, 630–637 (2006)CrossRef

47.170.

R.M. Glaeser, K. Downing, D. DeRosier, W. Chiu, J. Frank: Electron Crystallography of Biological Macromolecules (Oxford Univ. Press, Oxford 2007)

Titel: Protein Crystal Growth Methods
verfasst von: Andrea E. Gutiérrez-Quezada
Roberto Arreguín-Espinosa
Abel Moreno
Verlag: Springer Berlin Heidelberg
Buch: Springer Handbook of Crystal Growth
Print ISBN: 978-3-540-74182-4

Electronic ISBN: 978-3-540-74761-1

Copyright-Jahr: 2010
DOI: https://doi.org/10.1007/978-3-540-74761-1_47

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