PMID:15213393
| Citation |
Tonozuka, T, Uechi, A, Mizuno, M, Ichikawa, K, Nishikawa, A and Sakano, Y (2004) Crystallization and preliminary X-ray analysis of Escherichia coli K12 YgjK protein, a member of glycosyl hydrolase family 63. Acta Crystallogr. D Biol. Crystallogr. 60:1284-5 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1107/S0907444904009631 |
| Keywords |
Crystallization; Crystallography, X-Ray; Escherichia coli K12/enzymology; Escherichia coli Proteins/chemistry; Molecular Sequence Data; N-Glycosyl Hydrolases/chemistry |
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