Crystallization and X-ray diffraction analysis of a catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus

Journal Article · Tue Aug 01 00:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106026157· OSTI ID:22360169

Mine, Shouhei; Nakamura, Tsutomu ^[1]; Hirata, Kunio ^[2]; Ishikawa, Kazuhiko; Hagihara, Yoshihisa; Uegaki, Koichi ^[1]

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1. National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka, Ikeda, Osaka 563-8577 (Japan)
2. RIKEN/SPring-8, Kouto 1-1-1, Sayo-cho, Sayo-gun, Hyogo 679-5148 (Japan)

The expression, purification and preliminary X-ray diffraction analysis of a catalytic domain of a chitinase from P. furiosus is reported. 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 P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 90.0, b = 92.8, c = 107.2 Å.

• OSTI ID: 22360169
• Journal Information: Acta Crystallographica. Section F, Vol. 62, Issue Pt 8; Other Information: PMCID: PMC2242910; PMID: 16880559; PUBLISHER-ID: bw5153; OAI: oai:pubmedcentral.nih.gov:2242910; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ESCHERICHIA COLI
PROTEINS
RESOLUTION
SPACE GROUPS
WIGGLER MAGNETS
X-RAY DIFFRACTION