1LZT

REFINEMENT OF TRICLINIC LYSOZYME

Summary for 1LZT

• Entry DOI: 10.2210/pdb1lzt/pdb
• Descriptor: HEN EGG WHITE LYSOZYME (2 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: 14331.16

Authors

Hodsdon, J.M.,Brown, G.M.,Sieker, L.C.,Jensen, L.H. (deposition date: 1985-04-01, release date: 1985-07-18, Last modification date: 2024-10-09)

Primary citation

Hodsdon, J.M.,Brown, G.M.,Sieker, L.C.,Jensen, L.H.
Refinement of triclinic lysozyme: I. Fourier and least-squares methods.
Acta Crystallogr.,Sect.B, 46:54-62, 1990

PubMed Abstract: X-ray diffraction data to 1.5 A resolution have been collected for triclinic crystals of hen egg white lysozyme. The triclinic model was derived from the tetragonal one by the rotation function and refined initially by Fo-Fc and differential difference syntheses against 2 A resolution data. Refinement was continued by differential difference cycles against the 1.5 A data until R was reduced to 0.220. Although the initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic error which affected primarily the high-resolution data. Refinement was continued against the corrected 2 A data by block-diagonal least squares. After five cycles the refinement was terminated at R = 0.254 because of the imminent availability of a preferred refinement program. Problems with the protein model, the solvent, and the interaction of the scale and thermal parameters are discussed. The experiences gained in this study are summarized.

PubMed: 2302326
DOI: 10.1107/S0108768189009183

Experimental method

X-RAY DIFFRACTION (1.97 Å)