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International
Tables for Crystallography Volume F Crystallography of biological molecules Edited by M. G. Rossmann and E. Arnold © International Union of Crystallography 2006 |
International Tables for Crystallography (2006). Vol. F. ch. 8.1, pp. 165-166
Section 8.1.8.5. Optimized anomalous dispersion (MAD), improved MIR data and `structural genomics'
aDepartment of Chemistry, University of Manchester, M13 9PL, England |
Rapid protein structure determination via the MAD method of seleno protein variants (Hendrickson et al., 1990![[link]](/graphics/greenarr.gif)
), as well as xenon pressure derivatives (Schiltz et al., 1997), and improved heavy-atom isomorphous replacement data are removing a major bottleneck in protein crystallography, that of phase determination. One example of a successful MAD study with an especially weak anomalous signal, from one selenium atom per 147 amino acids, undertaken at ESRF BM14, is that of van Montfort et al. (1998). At another extreme is the largest number of anomalous scatterer sites; for example, Turner et al. (1998), using the NSLS, reported the successful determination of 30 selenium atoms in 96 kDa of protein (one dimer) in the asymmetric unit using one-wavelength anomalous differences (at peak) as E values and `Shake n' Bake' (Miller et al., 1994), followed by MAD phasing from three-wavelength data and solvent flattening. Overall, as the number of protein structures in the Protein Data Bank doubles every few years (currently the number is 9000), the possibility of considering whole genome-level structure determinations arises (Chayen et al., 1996; Chayen & Helliwell, 1998). The human genome, the determination of the amino-acid sequence of which is currently underway, comprises some 100 000 proteins. Of these, some 40% are membrane bound and somewhat difficult to crystallize. A MAD protein crystal structure currently requires roughly 1 day of SR BM beamtime. A coordination of 20 SR instruments worldwide, or an SR machine devoted solely to the project, could make major progress in 20 years. This estimate assumes no further speeding up of the technique, such as would acrue with faster detectors like the pixel detector. The smaller yeast genome, comprising amino-acid sequences of 10 000 proteins, has recently been completed. The molecular-weight histogram peaks at 30 kDa. Assuming, on average, that one amino acid out of 56 is a methionine, it is clear that the MAD method, and six Se atoms on average for each protein, is a good match to the task. This approach, along with homology modelling and genetic alignment techniques, opens the immense potential for `structural genomics' as a basis for understanding and controlling disease (e.g. see Bugg et al., 1993). SR and crystallography are now intricately intertwined in their scientific futures and in facilities provision (Helliwell, 1998).
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