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2lzt
From Proteopedia
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. 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 Page seeded by OCA on Sun May 4 09:31:40 2008
