2ds3
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(New page: 200px<br /><applet load="2ds3" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ds3, resolution 1.78Å" /> '''Crystal structure of...)
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Revision as of 11:08, 23 January 2008
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Crystal structure of E. coli YgjK, a member of glycosyl hydrolase family 63
Overview
Processing alpha-glucosidase I, which is classified into glycosyl, hydrolase (GH) family 63, hydrolyzes an oligosaccharide precursor of, eukaryotic N-linked glycoproteins. Recently, many bacteria have been, reported to possess genes for proteins that are homologous to the GH, family 63 glucosidases. In this paper, Escherichia coli K12 YgjK protein, a member of GH family 63, was overexpressed, purified and crystallized, using the vapour-diffusion method. Diffraction data were collected to 1.8, A resolution and the crystal was found to belong to the monoclinic space, group P2(1), with unit-cell parameters a = 88.5, b = 137.1, c = 60.9 A, beta = 98.1 degrees. The V(M) value was determined to be 2.1 A(3) Da(-1), which corresponds to the presence of two protein molecules in the, asymmetric unit.
About this Structure
2DS3 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary X-ray analysis of Escherichia coli K12 YgjK protein, a member of glycosyl hydrolase family 63., Tonozuka T, Uechi A, Mizuno M, Ichikawa K, Nishikawa A, Sakano Y, Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1284-5. Epub 2004, Jun 22. PMID:15213393
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