Tables for
Volume C
Mathematical, physical and chemical tables
Edited by E. Prince

International Tables for Crystallography (2006). Vol. C, ch. 3.1, pp. 148-155

Chapter 3.1. Preparation, selection, and investigation of specimens

P. F. Lindleya

aESRF, Avenue des Martyrs, BP 220, F-38043 Grenoble CEDEX, France


Axelrod, H. J., Feher, G., Allen, J. P., Chirino, A. J., Day, M. W., Hsu, B. T. & Rees, D. C. (1994). Crystallization and X-ray structure determination of cytochrome c2 from rhodobacter sphaeroides in three crystal forms. Acta Cryst. D50, 596–602.
Bernard, Y., Degoy, S., Lefaucheux, F. & Robert, M. C. (1994). A gel-mediated feeding technique for protein crystal growth from hanging drops. Acta Cryst. D50, 504–507.
Bishop, A. C. (1972). An outline of crystal morphology, 3rd ed., Chap. 11, pp. 254–282. London: Hutchinson Scientific and Technical.
Blundell, T. L. & Johnson, L. N. (1976). Protein crystallography, Chap. 3, pp. 59–82. New York: Academic Press.
Britton, D. (1972). Estimation of twinning parameter for twins with exactly superposed reciprocal lattices. Acta Cryst. A28, 296–297.
Bunn, C. W. (1961). Chemical crystallography: an introduction to optical and X-ray methods, 2nd ed., Chaps. 2, 3, 4, pp. 11–106. Oxford University Press.
Carter, C. W. Jr & Carter, C. W. (1979). Protein crystallisation using incomplete factorial experiments. J. Biol. Chem. 254, 12219–12223.
Carter, C. W. Jr & Yin, Y. (1994). Quantitative analysis in the characterization and optimization of protein crystal growth. Acta Cryst. D50, 572–590.
Chayen, N. E., Shaw Stewart, P. D. & Baldock, P. (1994). New developments of the IMPAX small-volume automated crystallization system. Acta Cryst. D50, 456–458.
Chayen, N. E., Shaw Stewart, P. D., Maeder, D. L. & Blow, D. M. (1990). An automated system for micro-batch protein crystallization and screening. J. Appl. Cryst. 23, 297–302.
Cox, M. J. & Weber, P. C. (1987). Experiments with automated protein crystallization. J. Appl. Cryst. 20, 366–373.
Cudney, B., Patel, S. & McPherson, A. (1994). Crystallization of macromolecules and silica gels. Acta Cryst. D50, 479–483.
Diller, T. C., Shaw, A., Stura, E. A., Vacquier, V. D. & Stout, C. D. (1994). Acid pH crystallization of the basic protein lysin from the spermatozoa of red abalone (Haliotis refescens). Acta Cryst. D50, 627–631.
Ducruix, A. & Giegé, R. (1992). Editors. Crystallisation of nucleic acids and proteins: a practical approach. Oxford University Press.
Eiselé, J.-L. (1993). Preparation of protein crystallization buffers with a computer-controlled motorized pipette: PIPEX. J. Appl. Cryst. 26, 92–96.
Ferré-D'Amaré, A. R. & Burley, S. K. (1994). Use of dynamic light scattering to assess crystallisability of macromolecules and macromolecular assemblies. Structure, 2(5), 357–359.
Fisher, R. G. & Sweet, R. M. (1980). Treatment of diffraction data from protein crystals twinned by merohedry. Acta Cryst. A36, 755–760.
Forsythe, E., Ewing, F. & Pusey, M. (1994). Studies on tetragonal lysozyme crystal growth rates. Acta Cryst. D50, 614–619.
Garavito, R. M. & Picot, D. (1990). Methods: a companion to methods in enzymology, Vol. 1, pp. 57–69. New York: Academic Press.
García-Ruiz, J. M. & Moreno, A. (1994). Investigations on protein crystal growth by the gel acupuncture method. Acta Cryst. D50, 484–490.
Giegé, R. & Ducruix, A. (1992). Crystallisation of nucleic acids and proteins: a practical approach, edited by A. Ducruix & R. Giegé, pp. 1–15. Oxford University Press.
Giegé, R., Theobald-Dietrich, A. & Lorber, B. (1993). Novel trends in protein and nucleic acid crystallisation: biochemical and physico-chemical aspects. Data collection and processing. Proceedings of the CCP4 Study Weekend, edited by L. Sawyer, N. Isaacs & S. Bailey, pp. 12–19. SERC Daresbury Laboratory, Warrington WA4 4AD, England.
Gilliland, G. L., 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.
Hampton Research (1994). Crystallisation research tools, Vol. 4, No. 2. Hampton Research, 5225 Canyon Crest Drive, Suite 71–336, Riverside, CA 92597, USA.
Harlos, K. (1992). Micro-bridges for sitting-drop crystallizations. J. Appl. Cryst. 25, 536–538.
Hartshorne, N. H. & Stuart, A. (1960). Crystals and the polarising microscope, 3rd ed. London: Arnold.
Helliwell, J. R. (1992). Macromolecular crystallography with synchrotron radiation, Chap. 2, pp. 11–23. Cambridge University Press.
Helliwell, M., Kaucic, V., Cheetham, G. M. T., Harding, M. M., Kariuki, B. M. & Rizkallah, P. J. (1993). Structure determination from small crystals of two aluminophosphates, CrAPO-14 and SAPO-43. Acta Cryst. B49, 413–420.
Hennig, M. & Schlesier, B. (1994). Crystallization of seed globulins from legumes. Acta Cryst. D50, 627–631.
Hodeau, J. L., Tu, H. Y., Bordet, P., Fournier, T., Strobel, P., Marezio, M. & Chandrashekar, G. V. (1992). Structure and twinning of Sr3CuPtO6. Acta Cryst. B48, 1–11.
Jancarik, J. & Kim, S.-H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24, 409–411.
Jeffery, J. W. (1977). Methods in X-ray crystallography, pp. 441–443. London/New York: Academic Press.
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.
Ladd, M. F. C. & Palmer, R. A. (1985). Structure determination by X-ray crystallography, 2nd ed., Chap. 3, pp. 101–112. New York/London: Plenum.
Luft, J. & Cody, V. (1989). A simple capillary vapor diffusion apparatus for surveying macromolecular crystallization conditions. J. Appl. Cryst. 22, 396.
Luft, J. R., Arakali, S. V., Kirisits, M. J., Kalenik, J., Waarzak, I., Cody, V., Pangborn, W. A. & DeTitta, G. T. (1994). A macromolecular crystallization procedure employing diffusion cells of varying depths as reservoirs to tailor the time course of equilibration in hanging- and sitting-drop vapor-diffusion and microdialysis experiments. J. Appl. Cryst. 27, 443–452.
McDermott, G. (1993). Crystallisation of membrane proteins. Data collection and processing. Proceedings of the CCP4 Study Weekend, edited by L. Sawyer, N. Isaacs & S. Bailey, pp. 20–27. SERC Daresbury Laboratory, Warrington WA4 4AD, England.
MacGillavry, C. H. & Henry, N. F. M. (1962). Preliminary investigation and selection of crystals for X-ray study. International tables for X-ray crystallography, Vol. III, pp. 5–13. Birmingham: Kynoch Press.
McPherson, A. (1976). The growth and preliminary investigation of protein and nucleic acid crystals for X-ray diffraction. Methods Biochem. Anal. 25, 249–345.
McPherson, A. (1982). The preparation and analysis of protein crystals. New York: John Wiley.
McPherson, A. (1985a). Crystallisation of macromolecules: general principles. Methods in enzymology, Vol. 114, pp. 112–120. New York: Academic Press.
McPherson, A. (1985b). Crystallisation of proteins by variation of pH and temperature. Methods in enzymology, Vol. 114, pp. 125–127. New York: Academic Press.
McPherson, A. (1990). Current approaches to macromolecular crystallisation. Eur. J. Biochem. 189, 1–23.
Makarova, I. P., Verin, I. A. & Aleksandrov, K. S. (1993). Structure and twinning of RbLiCrO4 crystals. Acta Cryst. B49, 19–28.
Mikol, V., Rodeau, J.-L. & Giegé, R. (1989). Changes of pH during biomacromolecule crystallization by vapour diffusion using ammonium sulfate as the precipitant. J. Appl. Cryst. 22, 155–161.
Monaco, H. L. (1994). The use of ammonium succinate in protein crystallography. J. Appl. Cryst. 27, 1068.
Oldfield, T. J., Ceska, T. A. & Brady, R. L. (1991). A flexible approach to automated protein crystallization. J. Appl. Cryst. 24, 255–260.
Phillips, F. C. (1971). An introduction to crystallography, 4th ed., Chap. 7, pp. 171–193. Edinburgh: Oliver & Boyd.
Przybylska, M. (1989). A double cell for controlling nucleation and growth of protein crystals. J. Appl. Cryst. 22, 115–118.
Redinbo, M. R. & Yeates, T. O. (1993). Structure determination of plastocyanin from a specimen with a hemihedral twinning fraction of one-half. Acta Cryst. D49, 375–380.
Reynolds, R. A., Remington, S. J., Weaver, L. H., Fisher, R. G., Anderson, W. F., Ammon, H. L. & Matthews, B. W. (1985). Structure of a serine protease from rat mast cells determined from twinned crystals by isomorphous and molecular replacement. Acta Cryst. B41, 139–147.
Riekel, C. (1993). Beamline 1: microfocus beamline. In Annual Report of the European Synchrotron Radiation Facility, Grenoble, France.
Ries-Kautt, M. & Ducruix, A. (1992). Crystallisation of nucleic acids and proteins: a practical approach, edited by A. Ducruix & R. Giegé, pp. 195–218. 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., Provost, K. & Lefaucheux, F. (1992). Crystallisation of nucleic acids and proteins: a practical approach, edited by A. Ducruix & R. Giegé, pp. 127–143. Oxford University Press.
Sadaoui, N., Janin, J. & Lewit-Bentley, A. (1994). TAOS: an automated system for protein crystallization. J. Appl. Cryst. 27, 622–626.
Scarborough, G. A. (1994). Large single crystals of the nerospora crassa plasma membrane H+-ATPase: an approach to the crystallization of integral membrane proteins. Acta Cryst. D50, 643–649.
Schick, B. & Jurnak, F. (1994). Extension of the diffraction resolution of crystals. Acta Cryst. D50, 563–568.
Sica, F., Demasi, D., Mazzarella, L., Zagari, A., Capasso, S., Pearl, L. H., D'Auria, S., Raia, C. A. & Rossi, M. (1994). Elimination of twinning in crystals of sulfolobus solfataricus alcohol dehydrogenase holo-enzyme by growth in agarose gels. Acta Cryst. D50, 508–511.
Sluis, P. van der, Hezemans, A. M. F. & Kroon, J. (1989). Crystallization of low-molecular-weight compounds for X-ray crystallography. J. Appl. Cryst. 22, 340–344.
Soriano, T. M. B. & Fontecilla-Camps, J. C. (1993). ASTEC: an automated system for sitting-drop protein crystallization. J. Appl. Cryst. 26, 558–562.
Spangfort, M. D., Surin, B. P., Dixon, N. E. & Svensson, L. A. (1994). Internal symmetry of the molecular chaperone cpn60 (GroEL) determined by X-ray crystallography. Acta Cryst. D50, 591–595.
Stout, G. H. & Jensen, L. H. (1968). X-ray structure determination: a practical guide, Chap. 4, pp. 62–82. London: Macmillan.
Thaller, C., Eichelle, G., Weaver, L. H., Wilson, E., Karlsson, R. & Jansonius, J. N. (1985). Seed enlargement and repeated seeding. Methods in Enzymology, Vol. 114, pp. 132–135. New York: Academic Press.
Thatcher, D. R. (1993). Protein purification and analysis for crystallographic studies. Data collection and processing. Proceedings of the CCP4 Study Weekend, edited by L. Sawyer, N. Isaacs & S. Bailey, pp. 2–11. SERC Daresbury Laboratory, Warrington WA4 4AD, England.
Thiessen, M. 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.
Tipson, R. S. (1956). Techniques of organic chemistry, Vol. III, Part I, Chap. 3. New York: Interscience.
Tissen, J. T. W. M., Fraaije, J. G. E. M., Drenth, J. & Berendsen, H. J. C. (1994). Mesoscopic theories for protein crystal growth. Acta Cryst. D50, 569–571.