1lyd
From Proteopedia
CRYSTAL STRUCTURE OF T4-LYSOZYME GENERATED FROM SYNTHETIC CODING DNA EXPRESSED IN ESCHERICHIA COLI
Overview
The polypeptide produced by expressing a chemically synthesized gene coding for the amino-acid sequence of T4-lysozyme has been crystallized and subjected to X-ray diffraction. The crystal structure has been refined to a standard R-factor of 0.191 for data between 8 and 2 A resolution. The refined model is essentially the same as the well-known structure of wild-type T4-lysozyme determined previously by Matthews et al. (1987). Some small changes in the C-terminal region, which is important in maintaining the folded structure, have been noted. In addition to confirming that the synthetic gene product is very close to the wild type, this structure provides a benchmark for protein engineering experiments on the folding and the catalytic activity of this molecule by the method of gene synthesis.
About this Structure
1LYD is a Single protein structure of sequence from Enterobacteria phage t4. The following page contains interesting information on the relation of 1LYD with [Lysozyme]. Full crystallographic information is available from OCA.
Reference
Crystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli., Rose DR, Phipps J, Michniewicz J, Birnbaum GI, Ahmed FR, Muir A, Anderson WF, Narang S, Protein Eng. 1988 Oct;2(4):277-82. PMID:3074306 Page seeded by OCA on Sat May 3 00:25:19 2008
