Abstract
Students new to the protein X-ray crystallography laboratory may understandably be confused when colleagues discuss Fouriers and Pattersons or molecular replacement and molecular dynamics refinement. However, they understand immediately that the first requirement for protein structure determination is to grow suitable crystals. Without crystals there can be no X-ray structure determination of a protein! In this chapter we discuss the principles of protein crystal growth and as an exercise give the recipe for crystallizing the enzyme lysozyme. We shall also generate an X-ray diffraction picture of a lysozyme crystal. This will provide an introduction to X-ray diffraction. The chapter concludes with a discussion of the problems encountered.
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References
Protein crystallization is extensively discussed in: Ducruix, A. and Giegé, R. (1992). For the crystallization of membrane proteins, see Michel, H. (1990) and Sowadski (1994).
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Paul P. Ewald, 1888–1985, professor of physics at several universities in Europe and the United States, was the first to apply the reciprocal lattice and the sphere named after him to the interpretation of an X-ray diffraction pattern.
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© 1999 Springer Science+Business Media New York
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Drenth, J. (1999). Crystallizing a Protein. In: Principles of Protein X-ray Crystallography. Springer Advanced Texts in Chemistry. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-3092-0_1
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DOI: https://doi.org/10.1007/978-1-4757-3092-0_1
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4757-3094-4
Online ISBN: 978-1-4757-3092-0
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