Open AccessCrystallization and X‐ray diffraction analysis of a catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus
Author(s) -
Mine Shouhei,
Nakamura Tsutomu,
Hirata Kunio,
Ishikawa Kazuhiko,
Hagihara Yoshihisa,
Uegaki Koichi
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106026157
Subject(s) - pyrococcus furiosus , crystallography , crystallization , chitinase , diffraction , archaea , resolution (logic) , chemistry , materials science , gene , biochemistry , optics , physics , organic chemistry , artificial intelligence , computer science
The crystallization and preliminary X‐ray diffraction analysis of a catalytic domain of chitinase (PF1233 gene) from the hyperthermophilic archaeon Pyrococcus furiosus is reported. The recombinant protein, prepared using an Escherichia coli expression system, was crystallized by the hanging‐drop vapour‐diffusion method. An X‐ray diffraction data set was collected at the undulator beamline BL44XU at SPring‐8 to a resolution of 1.50 Å. The crystals belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 90.0, b = 92.8, c = 107.2 Å.