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来自纤维单胞菌的外切-β-1,4-葡聚糖酶和β-1,4-木聚糖酶Cex催化结构域的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the bacterium Cellulomonas fimi.

作者信息

Bedarkar S, Gilkes N R, Kilburn D G, Kwan E, Rose D R, Miller R C, Warren R A, Withers S G

机构信息

Ontario Cancer Institute, Toronto, Canada.

出版信息

J Mol Biol. 1992 Nov 20;228(2):693-5. doi: 10.1016/0022-2836(92)90852-b.

Abstract

Single crystals of the catalytic domain of Cex, an exo-beta-1,4-glucanase and beta-1,4-xylanase from the cellulolytic bacterium Cellulomonas fimi, have been grown in the presence of polyethylene glycol 4000 using the vapour diffusion technique. The crystals, which diffract to better than 2.0 A resolution, belong to space group P4(1)2(1)2 or P4(3)2(1)2 and have cell constants: a = b = 88.21 A, c = 81.10 A; alpha = beta = gamma = 90 degrees.

摘要

来自纤维单胞菌的外切-β-1,4-葡聚糖酶和β-1,4-木聚糖酶Cex催化结构域的单晶,已采用气相扩散技术在聚乙二醇4000存在的情况下生长出来。这些晶体的衍射分辨率优于2.0 Å,属于空间群P4(1)2(1)2或P4(3)2(1)2,其晶胞常数为:a = b = 88.21 Å,c = 81.10 Å;α = β = γ = 90°。

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