Literature DB >> 12925805

Crystallization and preliminary X-ray studies of xylanase 10B from Thermotoga maritima.

Takashi Kumasaka, Tomonori Kaneko, Chihiro Morokuma, Satoshi Nakamura, Nobuo Tanaka.   

Abstract

Xylanases catalyze the hydrolysis of the beta-1,4-glycosidic bonds of xylan, which is the second most abundant component of plant cell walls after cellulose. The recombinant xylanase 10B from Thermotoga maritima MSB8 was prepared and crystallized by the sitting-drop vapour-diffusion method using 40 mM zinc acetate, 20 mM MES buffer pH 6.0 and 3% ethanol. Intensity data were collected to 2.5 A resolution at beamline BL26B2 of SPring-8. Preliminary X-ray analysis showed that the crystal belongs to space group P2(1)2(1)2, with unit-cell parameters a = 77.3, b = 80.6, c = 58.2 A and one molecule per asymmetric unit.

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Year:  2003        PMID: 12925805     DOI: 10.1107/s0907444903015397

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  An expression-driven approach to the prediction of carbohydrate transport and utilization regulons in the hyperthermophilic bacterium Thermotoga maritima.

Authors:  Shannon B Conners; Clemente I Montero; Donald A Comfort; Keith R Shockley; Matthew R Johnson; Swapnil R Chhabra; Robert M Kelly
Journal:  J Bacteriol       Date:  2005-11       Impact factor: 3.490

  1 in total

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