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An Eye Lens Protein–Water Structure: 1.2 Å Resolution Structure of γB-Crystallin at 150 K by V. S. Kumaraswamy; P. F. Lindley; C. Slingsby; I. D. Glover is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is An Eye Lens Protein–Water Structure: 1.2 Å Resolution Structure of γB-Crystallin at 150 K about?

7B-crystallin is a structural protein of the eye lens with a role in the maintenance of an even distribution of protein and water over distances around the wavelength of light, preserving lens transparency. The structure of the 174-residue bovine protein has already been determined at room temperature to 1.47 A resolution. By flash freezing the protein crystals, data have now been collected to a nominal resolution limit of 1.2 A as radiation damage was essentially eliminated. The protein-water model has been refined against this data using the program RESTRAIN converging to an R factor of 18.5% with all data. Atomic positions are clearly indicated in the electron-density maps. Discrete bimodal disorder has been visualized for a few side chains. Out of a total of 498 water molecules present in the crystal asymmetric unit, 394 have been modelled and refined at unit occupancy. The solvent structure is extremely well ordered with an average B value of 23.4 A 2. Partially occupied sites have been identified where disorder in the protein induces concomitant disorder in the local solvent structure. The solvent structure covers 97% of the solvent-exposed surface of the protein in the cryst

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Author

V. S. Kumaraswamy; P. F. Lindley; C. Slingsby; I. D. Glover

Publisher

International Union of Crystallography; Blackwell Publishing Inc.; International Union of Crystallography (IUCr) (ISSN 0907-4449)

Published

1996

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)