International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 4.1, pp. 81-93   | 1 | 2 |
https://doi.org/10.1107/97809553602060000660

Chapter 4.1. General methods

R. Giegéa* and A. McPhersonb

aUnité Propre de Recherche du CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 rue René Descartes, F-67084 Strasbourg CEDEX, France, and bDepartment of Molecular Biology & Biochemistry, University of California at Irvine, Irvine, CA 92717, USA
Correspondence e-mail:  R.Giege@ibmc.u-strasbg.fr

References

Astier, J. P., Veesler, S. & Boistelle, R. (1998). Protein crystals orientation in a magnetic field. Acta Cryst. D54, 703–706.
Ataka, M., Katoh, E. & Wakayama, N. L. (1997). Magnetic orientation as a tool to study the initial stage of crystallization of lysozyme. J. Cryst. Growth, 173, 592–596.
Baldwin, E. T., Crumly, K. V. & Carter, C. W. (1986). Practical, rapid screening of protein crystallization conditions by dynamic light scattering. Biophys. J. 49, 47–48.
Bancel, P. A., Cajipe, V. B., Rodier, F. & Witz, J. (1998). Laser seeding for biomolecular crystallization. J. Cryst. Growth, 191, 537–544.
Berne, P. F., Doublié, S. & Carter, C. W. Jr (1999). Molecular biology for structural biology. In Crystallization of nucleic acids and proteins, edited by A. Ducruix & R. Giegé, 2nd ed. Oxford University Press.
Boggon, T. J., Chayen, N. E., Snell, E. H., Dong, J., Lautenschlager, P., Potthast, L., Siddons, D. P., Stojanoff, V., Gordon, E., Thompson, A. W., Zagalsky, P. F., Bi, R.-C. & Helliwell, J. R. (1998). Protein crystal movements and fluid flows during microgravity growth. Philos. Trans. R. Soc. London Ser. A, 356, 1045–1061.
Bonneté, F., Malfois, M., Finet, S., Tardieu, A., Lafont, S. & Veesler, S. (1997). Different tools to study interaction potentials in γ-crystallin solutions: relevance to crystal growth. Acta Cryst. D53, 438–447.
Bosch, R., Lautenschlager, P., Potthast, L. & Stapelmann, J. (1992). Experiment equipment for protein crystallization in µg facilities. J. Cryst. Growth, 122, 310–316.
Bott, R. R., Navia, M. A. & Smith, J. L. (1982). Improving the quality of protein crystals through purification by isoelectric focusing. J. Biol. Chem. 257, 9883–9886.
Carter, D. C., Lim, K., Ho, J. X., Wright, B. S., Twigg, P. D., Miller, T. Y., Chapman, J., Keeling, K., Ruble, J., Vekilov, P. G., Thomas, B. R., Rosenberger, F. & Chernov, A. A. (1999). Lower dimer impurity incorporation may result in higher perfection of HEWL crystal grown in µg – a case study. J. Cryst. Growth, 196, 623–637.
Chayen, N. E. (1996). A novel technique for containerless protein crystallization. Protein Eng. 9, 927–929.
Chayen, N. E. (1997). A novel technique to control the rate of vapour diffusion, giving larger protein crystals. J. Appl. Cryst. 30, 198–202.
Chayen, N. E., Boggon, T. J., Cassetta, A., Deacon, A., Gleichmann, T., Habash, J., Harrop, S. J., Helliwell, J. R., Nieh, Y. P., Peterson, M. R., Raftery, J., Snell, E. H., Hädener, A., Niemann, A. C., Siddons, D. P., Stojanoff, V., Thompson, A. W., Ursby, T. & Wulff, M. (1996). Trends and challenges in experimental macromolecular crystallography. Q. Rev. Biophys. 29, 227–278.
Chayen, N. E., Lloyd, L. F., Collyer, C. A. & Blow, D. M. (1989). Trigonal crystals of glucose isomerase require thymol for their growth and stability. J. Cryst. Growth, 97, 367–374.
Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L. & Blow, D. M. (1990). An automated system for micro-batch protein crystallisation and screening. J. Appl. Cryst. 23, 297–302.
Chernov, A. A. (1997a). Crystals built of biological macromolecules. Phys. Rep. 288, 61–75.
Chernov, A. A. (1997b). Protein versus conventional crystals: creation of defects. J. Cryst. Growth, 174, 354–361.
Chernov, A. A. (1999). Estimates of internal stress and related mosaicity in solution grown crystals: proteins. J. Cryst. Growth, 196, 524–534.
Christopher, G. K., Phipps, A. G. & Gray, R. J. (1998). Temperature-dependent solubility of selected proteins. J. Cryst. Growth, 191, 820–826.
Cole, T., Kathman, A., Koszelak, S. & McPherson, A. (1995). Determination of the local refractive index for protein and virus crystals in solution by Mach–Zehnder interferometry. Anal. Biochem. 231, 92–98.
Crossio, M.-P. & Jullien, M. (1992). Fluorescence study of precrystallization of ribonuclease A: effect of salts. J. Cryst. Growth, 122, 66–70.
Cudney, B., Patel, S. & McPherson, A. (1994). Crystallization of macromolecules in silica gels. Acta Cryst. D50, 479–483.
D'Arcy, A., Elmore, C., Stihle, M. & Johnston, J. E. (1996). A novel approach to crystallizing proteins under oil. J. Cryst. Growth, 168, 175–180.
Declercq, J.-P., Evrard, C., Carter, D. C., Wright, B. S., Etienne, G. & Parello, J. (1999). A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution. J. Cryst. Growth, 196, 595–601.
DeLucas, L. J., Long, M. M., Moore, K. M., Rosenblum, W. M., Bray, T. L., Smith, C., Carson, M., Narayana, S. V. L., Harrington, M. D., Carter, D., Clark, A. D. Jr, Nanni, R. G., Ding, J., Jacobo-Molina, A., Kamer, G., Hughes, S. H., Arnold, E., Einspahr, H. M., Clancy, L. L., Rao, G. S. J., Cook, P. F., Harris, B. G., Munson, S. H., Finzel, B. C., McPherson, A., Weber, P. C., Lewandowski, F. A., Nagabhushan, T. L., Trotta, P. P., Reichert, P., Navia, M. A., Wilson, K. P., Thomson, J. A., Richards, R. N., Bowersox, K. D., Meade, C. J., Baker, E. S., Bishop, S. P., Dunbar, B. J., Trinh, E., Prahl, J., Sacco, A. Jr & Bugg, C. E. (1994). Recent results and new developments for protein crystal growth in microgravity. J. Cryst. Growth, 135, 183–195.
DeMattei, R. C. & Feigelson, R. S. (1992). Controlling nucleation in protein solutions. J. Cryst. Growth, 122, 21–30.
DeMattei, R. C. & Feigelson, R. S. (1993). Thermal methods for crystallizing biological macromolecules. J. Cryst. Growth, 128, 1225–1231.
Dobrianov, I., Finkelstein, K. D., Lemay, S. G. & Thorne, R. E. (1998). X-ray topographic studies of protein crystal perfection and growth. Acta Cryst. D54, 922–937.
Dock, A.-C., Lorber, B., Moras, D., Pixa, G., Thierry, J.-C. & Giegé, R. (1984). Crystallization of transfer ribonucleic acids. Biochimie, 66, 179–201.
Dock-Bregeon, A.-C., Chevrier, B., Podjarny, A., Moras, D., deBear, J. S., Gough, G. R., Gilham, P. T. & Johnson, J. E. (1988). High resolution structure of the RNA duplex [U(U–A)6A]2. Nature (London), 209, 375–378.
Dock-Bregeon, A.-C., Moras, D. & Giegé, R. (1999). Nucleic acids and their complexes. In Crystallization of nucleic acids and proteins, 2nd ed. A. Ducruix & R. Giegé, edited by Oxford University Press.
Ducruix, A. & Giegé, R. (1999). Editors. Crystallization of proteins and nucleic acids: a practical approach, 2nd ed. Oxford: IRL Press.
Ducruix, A., Guilloteau, J.-P., Riès-Kautt, M. & Tardieu, A. (1996). Protein interactions as seen by solution X-ray scattering prior to crystallogenesis. J. Cryst. Growth, 168, 28–39.
Durbin, S. D. & Carlson, W. E. (1992). Lysozyme crystal growth studied by atomic force microscopy. J. Cryst. Growth, 122, 71–79.
Durbin, S. D. & Feher, G. (1990). Studies of crystal growth mechanisms by electron microscopy. J. Mol. Biol. 212, 763–774.
Durbin, S. D. & Feher, G. (1996). Protein crystallization. Annu. Rev. Phys. Chem. 47, 171–204.
Ebel, C., Faou, P. & Zaccaï, G. (1999). Protein–solvent and weak protein–protein interactions in halophilic malate dehydrogenase. J. Cryst. Growth, 196, 395–402.
Ferré-D'Amaré, A. & Burley, S. K. (1997). Dynamic light scattering in evaluating crystallizability of macromolecules. Methods Enzymol. 276, 157–166.
Finet, S., Bonneté, F., Frouin, J., Provost, K. & Tardieu, A. (1998). Lysozyme crystal growth, as observed by small angle X-ray scattering, proceeds without crystallization intermediates. Eur. Biophys. J. 76, 554–561.
Fitzgerald, P. M. D. & Madson, N. B. J. (1986). Improvement of limit of diffraction and useful X-ray lifetime of crystals of glycogen debranching enzyme. J. Cryst. Growth, 76, 600–606.
Fourme, R., Ducruix, A., Ries-Kautt, M. & Capelle, B. (1995). The perfection of protein crystals probed by direct recording of Bragg reflection profiles with a quasi-planar X-ray wave. J. Synchrotron Rad. 2, 136–142.
García-Ruiz, J. M. & Moreno, A. (1994). Investigations on protein crystal growth by the gel acupuncture method. Acta Cryst. D50, 484–490.
García-Ruiz, J. M., Moreno, A., Otalora, F., Rondon, D., Viedma, C. & Zauscher, F. (1998). Teaching protein crystallization by the gel acupuncture method. J. Chem. Educ. 75, 442–446.
García-Ruiz, J. M., Novella, M. L. & Otalora, F. (1999). Supersaturation patterns in counter-diffusion crystallization methods followed by Mach–Zehnder interferometry. J. Cryst. Growth, 196, 703–710.
García-Ruiz, J. M. & Otalora, F. (1997). Crystal growth studies in microgravity with the APCF. II. Image analysis studies. J. Cryst. Growth, 182, 155–167.
Georgalis, Y., Zouni, A., Eberstein, W. & Saenger, W. (1993). Formation dynamics of protein precrystallization fractal clusters. J. Cryst. Growth, 126, 245–260.
George, A., Chiang, Y., Guo, B., Abrabshahi, A., Cai, Z. & Wilson, W. W. (1997). Second virial coefficient as predictor in protein crystal growth. Methods Enzymol. 276, 100–110.
Giegé, R., Dock, A.-C., Kern, D., Lorber, B., Thierry, J.-C. & Moras, D. (1986). The role of purification in the crystallization of proteins and nucleic acids. J. Cryst. Growth, 76, 554–561.
Giegé, R., Drenth, J., Ducruix, A., McPherson, A. & Saenger, W. (1995). Crystallogenesis of biological macromolecules. Biological, microgravity, and other physico-chemical aspects. Prog. Cryst. Growth Charact. 30, 237–281.
Giegé, R., Moras, D. & Thierry, J.-C. (1977). Yeast transfer RNAAsp: a new high resolution X-ray diffracting crystal form of a transfer RNA. J. Mol. Biol. 115, 91–96.
Gilliland, G., Tung, M., Blakeslee, D. M. & Ladner, J. E. (1994). Biological macromolecule crystallization database, version 3.0: new features, data and the NASA archive for protein crystal growth data. Acta Cryst. D50, 408–413.
Green, A. A. & Hughes, W. L. (1995). Protein fractionation on the basis of solubility in aqueous solutions of salts and organic solvents. Methods Enzymol. 1, 67–90.
Gripon, C., Legrand, L., Rosenman, I., Vidal, O., Robert, M.-C. & Boué, F. (1997). Lysozyme–lysozyme interactions in under- and super-saturated solutions: a simple relation between the second virial coefficient in H2O and D2O. J. Cryst. Growth, 178, 575–584.
Haas, C. & Drenth, J. (1998). The protein–water phase diagram and the growth of protein crystals from aqueous solution. J. Phys. Chem. 102, 4226–4232.
Hampel, A., Labananskas, M., Conners, P. G., Kirkegard, L., Raj Bhandary, U. L., Sigler, P. B. & Bock, R. M. (1968). Single crystals of transfer RNA from formyl-methionine and phenylalanine transfer RNA's. Science, 162, 1384–1386.
Harlos, K. (1992). Micro-bridges for sitting-drop crystallizations. J. Appl. Cryst. 25, 536–538.
Henisch, H. K. (1988). Crystals in gels and Liesegang rings. Cambridge, MA: Cambridge University Press.
Hilgenfeld, R., Liesum, A., Storm, R. & Plaas-Link, A. (1992). Crystallization of two bacterial enzymes on an unmanned space mission. J. Cryst. Growth, 122, 330–336.
Hirschler, J., Charon, M.-H. & Fontecilla-Camps, J. C. (1995). The effects of filtration on protein nucleation in different growth media. Protein Sci. 4, 2573–2577.
Izumi, K., Sawamura, S. & Ataka, M. (1996). X-ray topography of lysozyme crystals. J. Cryst. Growth, 168, 106–111.
Jakoby, W. B. (1971). Crystallization as a purification technique. Methods Enzymol. 22, 248–252.
Jerusalmi, D. & Steitz, T. A. (1997). Use of organic cosmotropic solutes to crystallize flexible proteins: application to T7 RNA polymerase and its complex with the inhibitor T7 lysozyme. J. Mol. Biol. 274, 748–756.
Judge, R. A., Forsythe, E. L. & Pusey, M. L. (1998). The effect of protein impurities on lysozyme crystal growth. Biotech. Bioeng. 59, 776–785.
Jurnak, F. (1986). Effect of chemical impurities in polyethylene glycol on macromolecular crystallization. J. Cryst. Growth, 76, 577–582.
Kam, Z., Shore, H. B. & Feher, G. (1978). On the crystallization of proteins. J. Mol. Biol. 123, 539–555.
Karpukhina, S. Ya., Barynin, V. V. & Lobanova, G. M. (1975). Crystallization of catalase in the ultracentrifuge. Sov. Phys. Crystallogr. 20, 417–418.
Kimble, W. L., Paxton, T. E., Rousseau, R. W. & Sambanis, A. (1998). The effect of mineral substrates on the crystallization of lysozyme. J. Cryst. Growth, 187, 268–276.
Komatsu, H., Miyashita, S. & Suzuki, Y. (1993). Interferometric observation of the interfacial concentration gradient layers around a lysozyme crystal. Jpn. J. Appl. Phys. 32(2), 1855–1857.
Konnert, J. H., D'Antonio, P. & Ward, K. B. (1994). Observation of growth steps, spiral dislocations and molecular packing on the surface of lysozyme crystals with the atomic force microscope. Acta Cryst. D50, 603–613.
Koszelak, S., Day, J., Leja, C., Cudney, R. & McPherson, A. (1995). Protein and virus crystal growth on International Microgravity Laboratory-2. Biophys. J. 69, 13–19.
Koszelak, S. & McPherson, A. (1988). Time lapse microphotography of protein crystal growth using a color VRC. J. Cryst. Growth, 90, 340–343.
Koszelak, S., Martin, D., Ng, J. & McPherson, A. (1991). Protein crystal growth rates determined by time lapse microphotography. J. Cryst. Growth, 110, 177–181.
Kurihara, K., Miyashita, S., Sazaki, G., Nakada, T., Suzuki, Y. & Komatsu, H. (1996). Interferometric study on the crystal growth of tetragonal lysozyme crystal. J. Cryst. Growth, 166, 904–908.
Kuznetsov, Y. G., Malkin, A. J., Greenwood, A. & McPherson, A. (1995). Interferometric studies of growth kinetics and surface morphology in macromolecular crystal growth: canavalin, thaumatin, and turnip yellow mosaic virus. J. Struct. Biol. 114, 184–196.
Lenhoff, A. M., Pjura, P. E., Dilmore, J. G. & Godlewski, T. S. Jr (1997). Ultracentrifugal crystallization of proteins: transport-kinetic modelling, and experimental behavior of catalase. J. Cryst. Growth, 180, 113–126.
Lorber, B. & Giegé, R. (1992). A versatile reactor for temperature controlled crystallization of biological macromolecules. J. Cryst. Growth, 122, 168–175.
Lorber, B. & Giegé, R. (1996). Containerless protein crystallization in floating drops: application to crystal growth monitoring under reduced nucleation conditions. J. Cryst. Growth, 168, 204–215.
Lorber, B. & Giegé, R. (1999). Biochemical aspects of macromolecular solutions and crystals. In Crystallization of nucleic acids and proteins, edited by A. Ducruix & R. Giegé, 2nd ed. Oxford University Press.
Lorber, B., Jenner, G. & Giegé, R. (1996). Effect of high hydrostatic pressure on nucleation and growth of protein crystals. J. Cryst. Growth, 158, 103–117.
Luft, J. R., Albright, D. T., Baird, J. K. & DeTitta, G. T. (1996). The rate of water equilibration in vapor-diffusion crystallizations: dependance on the distance from the droplet to the reservoir. Acta Cryst. D52, 1098–1106.
Luft, J. & Cody, V. (1989). A simple capillary vapor diffusion apparatus for surveying macromolecular crystallization conditions. J. Appl. Cryst. 22, 396.
Luft, J. R., Cody, V. & DeTitta, G. T. (1992). Experiences with HANGMAN: a macromolecular hanging drop vapor diffusion technique. J. Cryst. Growth, 122, 181–185.
Luft, J. R., Rak, D. M. & DeTitta, G. T. (1999a). Microbatch macromolecular crystallization in micropipettes. J. Cryst. Growth, 196, 450–455.
Luft, J. R., Rak, D. M. & DeTitta, G. T. (1999b). Microbatch macromolecular crystallization on a thermal gradient. J. Cryst. Growth, 196, 447–449.
McPherson, A. (1976). Crystallization of proteins from polyethylene glycol. J. Biol. Chem. 251, 6300–6303.
McPherson, A. (1982). The preparation and analysis of protein crystals. New York: John Wiley and Sons.
McPherson, A. (1990). Current approaches to macromolecular crystallization. Eur. J. Biochem. 189, 1–23.
McPherson, A. (1996). Macromolecular crystal growth in microgravity. Crystallogr. Rev. 6, 157–305.
McPherson, A. (1998). Crystallization of biological macromolecules. Cold Spring Harbor and New York: Cold Spring Harbor Laboratory Press.
McPherson, A., Malkin, A. J. & Kuznetsov, Y. G. (1995). The science of macromolecular crystallization. Structure, 3, 759–768.
McPherson, A., Malkin, A. J., Kuznetsov, Y. G. & Koszelak, S. (1996). Incorporation of impurities into macromolecular crystals. J. Cryst. Growth, 168, 74–92.
McPherson, A. & Shlichta, P. (1988). Heterogeneous and epitaxial nucleation of protein crystals on mineral surfaces. Science, 239, 385–387.
Malkin, A. J., Cheung, J. & McPherson, A. (1993). Crystallization of satellite tobacco mosaic virus. I. Nucleation phenomena. J. Cryst. Growth, 126, 544–554.
Malkin, A. J., Kuznetsov, Yu. G., Land, T. A., DeYoreo, J. J. & McPherson, A. (1995). Mechanisms of growth for protein and virus crystals. Nature Struct. Biol. 2, 956–959.
Malkin, A. J., Kuznetsov, Yu. G. & McPherson, A. (1996). Defect structure of macromolecular crystals. J. Struct. Biol. 117, 124–137.
Malkin, A. J. & McPherson, A. (1993). Light scattering investigations of protein and virus crystal growth: ferritin, apoferritin and satellite tobacco mosaic virus. J. Cryst. Growth, 128, 1232–1235.
Malkin, A. J. & McPherson, A. (1994). Light-scattering investigations of nucleation processes and kinetics of crystallization in macromolecular systems. Acta Cryst. D50, 385–395.
Matthews, B. W. (1985). Determination of protein molecular weight, hydration, and packing from crystal density. Methods Enzymol. 114, 176–187.
Mikol, V., Hirsch, E. & Giegé, R. (1990). Diagnostic of precipitant for biomacromolecule crystallization by quasi-elastic light scattering. J. Mol. Biol. 213, 187–195.
Mikol, V., Rodeau, J.-L. & Giegé, R. (1989). Changes of pH during biomacromolecule crystallization by vapor diffusion using ammonium sulfate as the precipitant. J. Appl. Cryst. 22, 155–161.
Mikol, V., Rodeau, J.-L. & Giegé, R. (1990). Experimental determination of water equilibrium rates in the hanging drop method of protein crystallization. Anal. Biochem. 186, 332–339.
Miller, T. V., He, X. M. & Carter, D. C. (1992). A comparison between protein crystals grown with vapor diffusion methods in microgravity and protein crystals using a gel liquid–liquid diffusion ground based method. J. Cryst. Growth, 122, 306–309.
Minezaki, Y., Nimura, N., Ataka, M. & Katsura, T. (1996). Small angle neutron scattering from lysozyme solutions in unsaturated and supersaturated states (SANS from lysozyme solutions). Biophys. Chem. 58, 355–363.
Nakada, T., Sazaki, G., Miyashita, S., Durbin, S. D. & Komatsu, H. (1999). Impurity effects on lysozyme crystallization as directly observed by atomic force microscopy. J. Cryst. Growth, 196, 503–510.
Neal, B. L., Asthagiri, D., Velev, O. D., Lenhoff, A. M. & Kaler, E. W. (1999). Why is the osmotic second virial coefficient related to protein crystallization? J. Cryst. Growth, 196, 377–387.
Ng, J., Kuznetsov, Y. G., Malkin, A. J., Keith, G., Giegé, R. & McPherson, A. (1997). Vizualization of RNA crystals growth by atomic force microscopy. Nucleic Acids Res. 25, 2582–2588.
Ng, J., Lorber, B., Witz, J., Théobald-Dietrich, A., Kern, D. & Giegé, R. (1996). The crystallization of biological macromolecules from precipitates. Evidence for Ostwald ripening. J. Cryst. Growth, 168, 50–62.
Ng, J. D., Lorber, B., Giegé, R., Koszelak, S., Day, J., Greenwood, A. & McPherson, A. (1997). Comparative analysis of thaumatin crystals grown on earth and in microgravity. Acta Cryst. D53, 724–733.
Otalora, F. & García-Ruiz, J. M. (1997). Crystal growth studies in microgravity with APCF. I. Computer simulation of transport dynamics. J. Cryst. Growth, 182, 141–154.
Otalora, F., García-Ruiz, J. M., Gavira, J. A. & Capelle, B. (1999). Topography and high resolution diffraction studies in tetragonal lysozyme. J. Cryst. Growth, 196, 546–558.
Papanikolau, Y. & Kokkinidis, M. (1997). Solubility, crystallization and chromatographic properties of macromolecules strongly depend on substances that reduce the ionic strength of the solution. Protein Eng. 10, 847–850.
Peters, R., Georgalis, Y. & Saenger, W. (1998). Accessing lysozyme nucleation with a novel dynamic light scattering detector. Acta Cryst. D54, 873–877.
Plester, V., Stapelmann, J., Potthast, L. & Bosch, R. (1999). The protein crystallization facility, a new European instrument to investigate biological macromolecular crystal growth on board the International Space Station. J. Cryst. Growth, 196, 638–648.
Price, S. R. & Nagai, K. (1995). Protein engineering as a tool for crystallography. Curr. Opin. Biotechnol. 6, 425–430.
Pronk, S. E., Hofstra, H., Groendijk, H., Kingma, J., Swarte, M. B. A., Dorner, F., Drenth, J., Hol, W. G. J. & Witholt, B. (1985). Heat-labile enterotoxin of Escherichia coli. Characterization of different crystal forms. J. Biol. Chem. 260, 13580–13584.
Provost, K. & Robert, M.-C. (1995). Crystal growth of lysozymes in media contaminated by parent molecules: influence of gelled media. J. Cryst. Growth, 156, 112–120.
Pusey, M., Witherow, W. K. & Nauman, R. (1988). Preliminary investigations into solutal flow about growing tetragonal lysozyme crystals. J. Cryst. Growth, 90, 105–111.
Pusey, M. L. (1993). A computer-controlled microscopy system for following protein crystal growth rates. Rev. Sci. Instrum. 64, 3121–3125.
Ray, W. J. Jr & Puvathingal, J. M. (1985). A simple procedure for removing contaminating aldehydes and peroxides from aqueous solutions of polyethylene glycols and of nonionic detergents that are based on the polyoxyethylene linkage. Anal. Biochem. 146, 307–312.
Rhim, W.-K. & Chung, S. K. (1990). Isolation of crystallizing droplets by electrostatic levitation. Methods Companion Methods Enzymol. 1, 118–127.
Richard, B., Bonneté, F., Dym, O. & Zaccaï, G. (1995). Archaea, a laboratory manual, pp. 149–154. Cold Spring Harbor Laboratory Press.
Riès-Kautt, M. & Ducruix, A. (1991). Crystallization of basic proteins by ion pairing. J. Cryst. Growth, 110, 20–25.
Riès-Kautt, M. & Ducruix, A. (1999). Phase diagrams. In Crystallization of nucleic acids and proteins, edited by A. Ducruix & R. Giegé, 2nd ed. Oxford University Press.
Robert, M. C., Bernard, Y. & Lefaucheux, F. (1994). Study of nucleation-related phenomena in lysozyme solutions. Application to gel growth. Acta Cryst. D50, 496–503.
Robert, M.-C. & Lefaucheux, F. (1988). Crystal growth in gels: principles and applications. J. Cryst. Growth, 90, 358–367.
Robert, M.-C., Vidal, O., García-Ruiz, J. M. & Otalora, F. (1999). Crystallization in gels and related methods. In Crystallization of nucleic acids and proteins, edited by A. Ducruix & R. Giegé, 2nd ed. Oxford University Press.
Rosenberger, F. (1996). Protein crystallization. J. Cryst. Growth, 166, 40–54.
Rosenberger, F., Vekilov, P. G., Muschol, M. & Thomas, B. R. (1996). Nucleation and crystallization of globular proteins – what do we know and what is missing. J. Cryst. Growth, 168, 1–27.
Rossi, G. L. (1992). Biological activity in the crystalline state. Curr. Opin. Struct. Biol. 2, 816–820.
Salemme, F. R. (1972). A free interface diffusion technique for crystallization of proteins for X-ray crystallography. Arch. Biochem. Biophys. 151, 533–540.
Sauter, C., Lorber, B., Kern, D., Cavarelli, J., Moras, D. & Giegé, R. (1999). Crystallogenesis studies on yeast aspartyl-tRNA synthetase: use of phase diagram to improve crystal quality. Acta Cryst. D55, 149–156.
Sauter, C., Ng, J. D., Lorber, B., Keith, G., Brion, P., Hosseini, M. W., Lehn, J.-M. & Giegé, R. (1999). Additives for the crystallization of proteins and nucleic acids. J. Cryst. Growth, 196, 365–376.
Sazaki, G., Yoshida, E., Komatsu, H., Nakada, T., Miyashita, S. & Watanabe, K. (1997). Effects of a magnetic field on the nucleation and growth of protein crystals. J. Cryst. Growth, 173, 231–234.
Shlichta, P. J. (1986). Feasibility of mapping solution properties during the growth of protein crystals. J. Cryst. Growth, 76, 656–662.
Shu, Z.-Y., Gong, H.-Y. & Bi, R.-C. (1998). In situ measurements and dynamic control of the evaporation rate in vapor diffusion crystallization of proteins. J. Cryst. Growth, 192, 282–289.
Skouri, M., Lorber, B., Giegé, R., Munch, J.-P. & Candau, S. J. (1995). Effect of macromolecular impurities on lysozyme solubility and crystallizability. Dynamic light scattering, phase diagram, and crystal growth studies. J. Cryst. Growth, 152, 209–220.
Snell, E., Helliwell, J. R., Boggon, T. J., Lautenschlager, P. & Potthast, L. (1996). First ground trials of a Mach–Zehnder interferometer for implementation into a microgravity protein crystallization facility – the APCF. Acta Cryst. D52, 529–533.
Snell, E. H., Weisgerber, S., Helliwell, J. R., Weckert, E., Hölzer, K. & Schroer, K. (1995). Improvements in lysozyme protein crystal perfection through microgravity growth. Acta Cryst. D51, 1099–1102.
Sousa, R., Lafer, E. M. & Wang, B.-C. (1991). Preparation of crystals of T7 RNA polymerase suitable for high resolution X-ray structure analysis. J. Cryst. Growth, 110, 237–246.
Stojanoff, V., Siddons, D. P., Monaco, L. A., Vekilov, P. & Rosenberger, F. (1997). X-ray topography of tetragonal lysozyme grown by the temperature-controlled technique. Acta Cryst. D53, 588–595.
Stojanoff, V., Snell, E. F., Siddons, D. P. & Helliwell, J. R. (1996). An old technique with a new application: X-ray topography of protein crystals. Synchrotron Radiat. News, 9, 25–26.
Strickland, C. L., Puchalski, R., Savvides, S. N. & Karplus, P. A. (1995). Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry. Acta Cryst. D51, 337–341.
Stura, E. A. & Wilson, I. A. (1990). Analytical and production seeding techniques. Methods Companion Methods Enzymol. 1, 38–49.
Suzuki, Y., Miyashita, S., Komatsu, H., Sato, K. & Yagi, T. (1994). Crystal growth of hen egg white lysozyme under high pressure. Jpn. J. Appl. Phys. 33, 1568–1570.
Sygusch, J., Coulombe, R., Cassanto, J. M., Sportiello, M. G. & Todd, P. (1996). Protein crystallization in low gravity by step gradient diffusion method. J. Cryst. Growth, 162, 167–172.
Taleb, M., Didierjean, C., Jelsch, C., Mangeot, J.-P., Capelle, B. & Aubry, A. (1999). Crystallization of biological macromolecules under an external electric field. J. Cryst. Growth, 200, 575–582.
Thaller, D., Eichele, G., Weaver, L. H., Wilson, E., Karlsson, R. & Jansonius, J. N. (1985). Seed enlargement and repeated seeding. Methods Enzymol. 114, 132–135.
Thibault, F., Langowski, L. & Leberman, R. (1992). Pre-nucleation crystallization studies on aminoacyl-tRNA synthetases by dynamic light scattering. J. Mol. Biol. 225, 185–191.
Thiessen, K. J. (1994). The use of two novel methods to grow protein crystals by microdialysis and vapor diffusion in an agarose gel. Acta Cryst. D50, 491–495.
Thomas, B. R., Vekilov, P. G. & Rosenberger, F. (1998). Effects of microheterogeneity in hen egg-white lysozyme crystallization. Acta Cryst. D54, 226–236.
Thomas, D. H., Rob, A. & Rice, D. W. (1989). A novel dialysis procedure for the crystallization of proteins. Protein Eng. 2, 489–491.
Timasheff, S. N. & Arakawa, T. (1988). Mechanism of protein precipitation and stabilization by co-solvents. J. Cryst. Growth, 90, 39–46.
Vaney, M. C., Maignan, S., Riès-Kautt, M. & Ducruix, A. (1996). High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Cryst. D52, 505–517.
Vekilov, P. G., Ataka, M. & Katsura, T. (1992). Laser Michelson interferometry investigation of protein crystal growth. J. Cryst. Growth, 130, 317–320.
Vekilov, P. G. & Rosenberger, F. (1996). Dependence of lysozyme growth kinetics on step sources and impurities. J. Cryst. Growth, 158, 540–551.
Vekilov, P. G. & Rosenberger, F. (1998). Protein crystal growth under forced solution flow: experimental setup and general response of lysozyme. J. Cryst. Growth, 186, 251–261.
Vidal, O., Robert, M.-C. & Boué, F. (1998a). Gel growth of lysozyme crystals studied by small angle neutron scattering: case of agarose gel, a nucleation promotor. J. Cryst. Growth, 192, 257–270.
Vidal, O., Robert, M.-C. & Boué, F. (1998b). Gel growth of lysozyme crystals studied by small angle neutron scattering: case of silica gel, a nucleation inhibitor. J. Cryst. Growth, 192, 271–281.
Vuillard, L., Rabilloud, T., Leberman, R., Berthet-Colominas, C. & Cusack, S. (1994). A new additive for protein crystallization. FEBS Lett. 353, 294–296.
Weber, B. H. & Goodkin, P. E. (1970). A modified microdiffusion procedure for the growth of single protein crystals by concentration-gradient equilibrium dialysis. Arch. Biochem. Biophys. 141, 489–498.
Yonath, A., Müssig, J. & Wittmann, H. G. (1982). Parameters for crystal growth of ribosomal subunits. J. Cell. Biochem. 19, 145–155.
Zeppenzauer, M. (1971). Formation of large crystals. Methods Enzymol. 22, 253–266.