Open AccessExpression, crystallization and preliminary X‐ray diffraction studies of thermostable β‐1,3‐xylanase from Thermotoga neapolitana strain DSM 4359
Author(s) -
Okazaki Fumiyoshi,
Ogino Chiaki,
Kondo Akihiko,
Mikami Bunzo,
Kurebayashi Yoichi,
Tsuruta Hiroki
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111017222
Subject(s) - xylanase , thermotoga maritima , crystallography , crystallization , strain (injury) , resolution (logic) , materials science , diffraction , x ray crystallography , chemistry , biology , biochemistry , enzyme , optics , organic chemistry , physics , escherichia coli , anatomy , artificial intelligence , computer science , gene
Crystals of β‐1,3‐xylanase (1,3‐β‐ d ‐xylan xylanohydrolase; EC 3.2.1.32) from Thermotoga neapolitana strain DSM 4359 with maximum dimensions of 0.2 × 0.1 × 0.02 mm were grown using the sitting‐drop vapour‐diffusion method at 293 K over 24 h. The crystals diffracted to a resolution of 1.82 Å, allowing structure determination. The crystals belonged to space group P 2 1 , with unit‐cell parameters a = 39.061, b = 75.828, c = 52.140 Å; each asymmetric unit cell contained a single molecule.