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X-ray crystallography proteins

Drenth J. Principles of Protein X-Ray Crystallography. New York Springer-Verlag, 1994. [Pg.30]

Figure 3.4 X-ray beam passing through the Ewald sphere and diffracted by planes in a single crystal produces reflection spots. (Adapted with permission from Figure 1.13 of Drenth, J. Principles of Protein X-ray Crystallography, 2nd ed., Springer-Verlag, New York, 1999. Copyright 1999 Springer-Verlag, New York.)... Figure 3.4 X-ray beam passing through the Ewald sphere and diffracted by planes in a single crystal produces reflection spots. (Adapted with permission from Figure 1.13 of Drenth, J. Principles of Protein X-ray Crystallography, 2nd ed., Springer-Verlag, New York, 1999. Copyright 1999 Springer-Verlag, New York.)...
Structures of actual enzyme-substrate complexes are generally difficult to determine, because the reaction occurs too quickly, but techniques now available occasionally enable study of these complexes [53]. Protein X-ray crystallography has several limitations, for example, it often gives little or no information about the positions of protons (because of the low electron density of hydrogen atoms) in a particular protein. This can cause prob-... [Pg.182]

Drenth, J. (1994), Principles of protein X-ray crystallography. New York Springer. [Pg.64]

Is protein X-ray crystallography a technique that can be used in your laboratory The easiest way to answer this question is to discuss what crystallography can do and the information that can (and cannot) be extracted from crystal structures. [Pg.457]

Protein X-ray crystallography gives a snapshot of the structure of a protein as it exists in a crystal. This technique provides a complete and unambiguous three-dimensional (3-D) representation of a protein molecule. It is important to note that the model generated from a crystallographic study is a static or time-averaged view of the molecular structure. Information about molecular motions can be obtained from precise diffraction data however, the motions of molecules within a crystal are usually severely restricted in comparison to the motions of molecules in solution. [Pg.457]

The theory behind protein X-ray crystallography is probably of limited interest to the majority of readers of this chapter, and this text will not go into a great deal of depth on the theory behind this technique. Only theory sufficient to discuss the practical side of crystallography will be introduced. For the few who are interested in a more in-depth understanding of the theory there are many excellent texts that deal with this subject in great detail. Some of these texts are listed under O Section 5. [Pg.459]

This hst of books is by no means considered an exhaustive list on protein X-ray crystallography. These are merely books that I have found useful, or have been recommended to me by colleagues. Other suggestions for additions to this hst will be gratefully received. [Pg.476]

Drenth, J. (1999). Principles of Protein X-ray Crystallography, 2nd edn. Springer-Verlag, Berlin. [Pg.94]


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See also in sourсe #XX -- [ Pg.172 , Pg.179 , Pg.186 ]




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