By John R. Helliwell
ISBN-10: 0511524269
ISBN-13: 9780511524264
ISBN-10: 0521334675
ISBN-13: 9780521334679
ISBN-10: 0521544041
ISBN-13: 9780521544047
This hugely illustrated monograph presents a finished research of the constitution and serve as of proteins, nucleic acids and viruses utilizing synchrotron radiation and crystallography. Synchrotron radiation is severe, polychromatic and finely collimated, and is extremely potent for probing the constitution of macromolecules. it is a fast-expanding box, and this well timed monograph supplies a whole advent to the strategy and its makes use of. starting with chapters at the basics of macromolecular crystallography and macromolecular constitution, the ebook is going directly to evaluate the assets and homes of synchrotron radiation, instrumentation and knowledge assortment. There are chapters at the Laue technique, on diffuse X-ray scattering and on variable wavelength dispersion tools. The ebook concludes with an outline and survey of purposes together with reports at excessive solution, using small crystals, the learn of enormous unit cells, and time-resolved crystallography (particularly of enzymes). Appendices are supplied which current crucial details for the synchrotron consumer in addition to information regarding synchrotron amenities presently on hand. an in depth bibliography and reference part completes the amount. Many tables, diagrams and pictures are incorporated.
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Extra info for Macromolecular Crystallography with Synchrotron Radiation
Example text
There is a wide selection of texts available which are listed in the bibliography. 1) where d is the interplanar spacing of that set of planes, A is the wavelength of the X-rays and n is an integer. For a fixed X, the closer the separation of the planes then the larger the value of 0, the diffraction angle; this corresponds to higher resolution data. 11(5)). The Laue equations can be recast by using the concept of the reciprocal lattice. New vectors a*, b* and c* can be defined by the following relationships: a-a* = l b-a* = 0 c-a* = O a-b* = 0 b-b* = l c-b* = 0 a-c* = 0 b-c* = 0 c-c* = l 1 f (2-3) J The vectors a*, b* and c* define a reciprocal lattice whereby the magnitude of a*, for example, is inversely related to a and likewise b* to b and c* to c.
Ii) Orthorhombic crystals of concanavalin-A (complexed with a-methyl mannoside). 5A, a=/3=y=90°. Photograph kindly provided by Dr J. Yariv with permission. (iii) Orthorhombic crystals of concanavalin-A (without saccharide). 1 A, a=£=y=90°. Typical size ~1 mm longest dimension. Photograph kindly provided by Dr J. Yariv with permission. 16 Fundamentals of macromolecular crystallography (v) (iv) Orthorhombic crystals of 6phosphogluconate dehydrogenase. 9A, a=p=y=90°. Typical largest dimension ~lmm.
Similarly bromine can be incorporated into a nucleotide. In all these cases data can be collected at multiple wavelengths using SR and this allows phases to be determined. Protein structures have now been solved by several variants of these methods. This is an important technical capability because it either reduces the number of heavy atom derivatives that need to be found for isomorphous replacement or allows phase determination from a single crystal. Future applications of SR in macromolecular crystallography involve extrapolations from the use of existing SR sources to the next generation of sources such as the European Synchrotron Radiation Facility (ESRF) in Grenoble or the Advanced Photon Source (APS) at Argonne or the Super Photon Ring (SPRING) in Japan.
Macromolecular Crystallography with Synchrotron Radiation by John R. Helliwell
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