Tables for
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F. ch. 23.4, pp. 637-638   | 1 | 2 |

Section Summary

C. Mattosa* and D. Ringeb

aDepartment of Molecular and Structural Biochemistry, North Carolina State University, 128 Polk Hall, Raleigh, NC 02795, USA, and  bRosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South St, Waltham, MA 02254, USA
Correspondence e-mail: Summary

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In general, small proteins serve as important models where results of X-ray crystallography, NMR and molecular-dynamics calculations can be easily compared and cross-validated, since larger proteins are more difficult to study by the latter two techniques. Small proteins are also more likely to form relatively ordered crystals, which are able to diffract X-rays to atomic resolution (of the order of 1 Å). With respect to understanding solvent structure, the two major contributions of these very high resolution protein models are the observation of solvent structure around hydrophobic residues, where at lower resolution the water molecules `look' disordered, and a glimpse at the pattern of water occupancy likely to occur on protein surfaces.

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