Structural highlights
Function
[CEXY_CLOSR] Active toward xylan, carboxymethylcellulose, P-nitrophenyl-beta-D-xylopyranoside and P-nitrophenyl-beta-D-cellobioside.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Recombinant mature xylanase B from Clostridium stercorarium has been prepared and crystallized by the sitting-drop vapour-diffusion method using 4 mg ml(-1) purified enzyme, 10.3%(w/v) polyethylene glycol 1500, 8.6%(v/v) glycerol and 0.34 M non-detergent sulfobetaine 195. A suitable crystal grew after incubation for ten weeks at 293 K. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 64.76, b = 96.60, c = 138.44 A. X-ray diffraction data were collected to 1.80 A resolution.
Crystallization and preliminary X-ray analysis of xylanase B from Clostridium stercorarium.,Nishimoto M, Fushinobu S, Miyanaga A, Wakagi T, Shoun H, Sakka K, Ohmiya K, Nirasawa S, Kitaoka M, Hayashi K Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):342-3. Epub 2004, Jan 23. PMID:14747719[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nishimoto M, Fushinobu S, Miyanaga A, Wakagi T, Shoun H, Sakka K, Ohmiya K, Nirasawa S, Kitaoka M, Hayashi K. Crystallization and preliminary X-ray analysis of xylanase B from Clostridium stercorarium. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):342-3. Epub 2004, Jan 23. PMID:14747719 doi:10.1107/S090744490302715X
