2lzt

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REFINEMENT OF TRICLINIC LYSOZYME. II. THE METHOD OF STEREOCHEMICALLY RESTRAINED LEAST-SQUARES

Structural highlights

2lzt is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.97Å
Ligands:NO3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Ramanadham M, Sieker LC, Jensen LH. Refinement of triclinic lysozyme: II. The method of stereochemically restrained least squares. Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):63-9. PMID:2302327

Contents


PDB ID 2lzt

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