193l
From Proteopedia
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THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME
Overview
Crystals of tetragonal hen egg-white lysozyme were grown using Advanced, Protein Crystallization Facility (APCF) apparatus under a microgravity, environment (SpaceHab-01 mission) and ground control conditions. Crystals, were grown from NaCl as a crystallizing agent at pH 4.3. The X-ray, diffraction patterns of the best diffracting ground- and space-grown, crystals were recorded using synchrotron radiation and an image plate on, the W32 beamline at LURE. Both ground- and space-grown crystals showed, nearly equivalent maximum resolution of 1.3-1.4 A. Refinements were, carried out with the program X-PLOR with final R values of 18.45 and, 18.27% for structures from ground- and space- grown crystals, respectively. The two structures are nearly identical with the, root-mean-square difference on all protein atoms being 0.13 A. Some, residues of the two refined structures show multiple alternative, conformations. Two ions were localized into the electron-density maps of, the two structures: one chloride ion at the interface between two, symmetry-related molecules and one sodium ion stabilizing the loop, Ser60-Leu75. The sodium ion is surrounded by six ligands which form a, bipyramid around it at distances of 2.2-2.6 A.
About this Structure
193L is a Single protein structure of sequence from Gallus gallus with CL and NA as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission., Vaney MC, Maignan S, Ries-Kautt M, Ducriux A, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):505-17. PMID:15299672
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