2vb1
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been | + | The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation. Refinement with anisotropic displacement parameters and with the removal of stereochemical restraints for the well ordered parts of the structure converged with a conventional R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. In addition to the 129-residue protein, a total of 170 water molecules, nine nitrate ions, one acetate ion and three ethylene glycol molecules were located in the electron-density map. Eight sections of the main chain and many side chains were modeled with alternate conformations. The occupancies of the water sites were refined and this step is meaningful when assessed by use of the free R factor. A detailed description and comparison of the structure are made with reference to the previously reported triclinic HEWL structures refined at 0.925 A (at the low temperature of 120 K) and at 0.95 A resolution (at room temperature). |
==About this Structure== | ==About this Structure== | ||
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[[Category: triclinic hewl]] | [[Category: triclinic hewl]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:54:44 2008'' |
Revision as of 16:54, 21 February 2008
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HEWL AT 0.65 ANGSTROM RESOLUTION
Overview
The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation. Refinement with anisotropic displacement parameters and with the removal of stereochemical restraints for the well ordered parts of the structure converged with a conventional R factor of 8.39% and an R(free) of 9.52%. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. In addition to the 129-residue protein, a total of 170 water molecules, nine nitrate ions, one acetate ion and three ethylene glycol molecules were located in the electron-density map. Eight sections of the main chain and many side chains were modeled with alternate conformations. The occupancies of the water sites were refined and this step is meaningful when assessed by use of the free R factor. A detailed description and comparison of the structure are made with reference to the previously reported triclinic HEWL structures refined at 0.925 A (at the low temperature of 120 K) and at 0.95 A resolution (at room temperature).
About this Structure
2VB1 is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Known structural/functional Sites: , , , , , , , , , , , and . Full crystallographic information is available from OCA.
Reference
Triclinic lysozyme at 0.65 A resolution., Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2007 Dec;63(Pt 12):1254-68. Epub 2007, Nov 16. PMID:18084073
Page seeded by OCA on Thu Feb 21 18:54:44 2008
Categories: Gallus gallus | Lysozyme | Single protein | Alkire, R. | Dauter, M. | Dauter, Z. | Joachimiak, A. | Wang, J. | ACT | EDO | NO3 | Allergen | Antimicrobial | Atomic resolution | Bacteriolytic enzyme | Glycosidase | Hydrolase | Triclinic hewl
