2LZT

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

Summary for 2LZT

• Entry DOI: 10.2210/pdb2lzt/pdb
• Descriptor: HEN EGG WHITE LYSOZYME, NITRATE ION (3 entities in total)
• Functional Keywords: hydrolase(o-glycosyl)
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14641.18

Authors

Ramanadham, M.,Sieker, L.C.,Jensen, L.H. (deposition date: 1989-08-21, release date: 1990-01-15, Last modification date: 2024-11-06)

Primary citation

Ramanadham, M.,Sieker, L.C.,Jensen, L.H.
Refinement of triclinic lysozyme: II. The method of stereochemically restrained least squares.
Acta Crystallogr.,Sect.B, 46:63-69, 1990

PubMed Abstract: 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.

PubMed: 2302327
DOI: 10.1107/S0108768189009195

Experimental method

X-RAY DIFFRACTION (1.97 Å)