2lzt
From Proteopedia
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REFINEMENT OF TRICLINIC LYSOZYME. II. THE METHOD OF STEREOCHEMICALLY RESTRAINED LEAST-SQUARES
Overview
Refinement of triclinic lysozyme by restrained least squares against the 2, A resolution X-ray data is described, beginning with the model from cycle, 17 of the preceding paper [Hodsdon, Brown, Sieker & Jensen (1990). Acta, Cryst. B46, 54-62]. After 20 refinement cycles, R stood at 0.172., Nevertheless, serious errors involving both main-chain and side-chain, atoms still remained, requiring numerous model rebuilding sessions, interleaved with refinement cycles. After 63 cycles R = 0.124 for the, model which includes all protein atoms, 249 water oxygen sites and five, nitrate ions. Although the overall B is relatively low, 10.5 A2, B's for, atoms in the region of residues 101-103, toward the termini of some of the, longer side chains, and in the region of the C terminus of the main chain, exceed 20 A2, indicating relatively high atomic mobilities, disorder, or, remaining errors in the model.
About this Structure
2LZT is a Single protein structure of sequence from Gallus gallus with NO3 as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Refinement of triclinic lysozyme: II. The method of stereochemically restrained least squares., Ramanadham M, Sieker LC, Jensen LH, Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):63-9. PMID:2302327
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