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1amm

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1amm, resolution 1.2Å

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1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K

Overview

gammabeta-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 crystal., 126 water molecules are distributed in second and higher hydration shells., There are networks of hydrogen-bonded solvent extending up to 64 molecules, in a network, comprising trimers and tetramers as well as five- and, six-membered water-ring structures. The hydration of the protein surface, is dominated by arginine and aspartate side chains. Extensive cages of, highly ordered solvent molecules are also observed around exposed, non-polar groups.

About this Structure

1AMM is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

An eye lens protein-water structure: 1.2 A resolution structure of gammaB-crystallin at 150 K., Kumaraswamy VS, Lindley PF, Slingsby C, Glover ID, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):611-22. PMID:15299624

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