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Title: Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis

Abstract

Glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis was crystallized and preliminary crystallographic studies of the crystals were performed. Glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis was crystallized and preliminary crystallographic studies of the crystals were performed. Crystals were grown at 293 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.4 Å resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 Å. Assuming the presence of two molecules in the asymmetric unit, the V{sub M} value was 2.7 Å{sup 3} Da{sup −1} and the solvent content was 54.1%. The protein was also cocrystallized with substrates and diffraction data were collected to 2.7 Å resolution.

Authors:
; ;  [1];  [2];  [3];  [1];  [3];  [1]
+ Show Author Affiliations
  1. Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871 (Japan)
  2. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871 (Japan)
  3. (Sosho Project), JST, 2-1 Yamadaoka, Suita, Osaka 565-0871 (Japan)
Publication Date:
OSTI Identifier:
22360258
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 2; Other Information: PMCID: PMC2330122; PMID: 17277457; PUBLISHER-ID: fw5119; OAI: oai:pubmedcentral.nih.gov:2330122; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; GLYCEROL; MOLECULES; PROTEINS; RESOLUTION; SOLVENTS; SPACE GROUPS; SUBSTRATES; SYNCHROTRON RADIATION; X-RAY DIFFRACTION

Citation Formats

Katsumi, Ryota, Koga, Yuichi, You, Dong-Ju, Matsumura, Hiroyoshi, CREST, Takano, Kazufumi, CREST, and Kanaya, Shigenori, E-mail: kanaya@mls.eng.osaka-u.ac.jp. Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107001388.
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Katsumi, Ryota, Koga, Yuichi, You, Dong-Ju, Matsumura, Hiroyoshi, CREST, Takano, Kazufumi, CREST, & Kanaya, Shigenori, E-mail: kanaya@mls.eng.osaka-u.ac.jp. Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis. United Kingdom. doi:10.1107/S1744309107001388.
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Katsumi, Ryota, Koga, Yuichi, You, Dong-Ju, Matsumura, Hiroyoshi, CREST, Takano, Kazufumi, CREST, and Kanaya, Shigenori, E-mail: kanaya@mls.eng.osaka-u.ac.jp. Thu . "Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis". United Kingdom. doi:10.1107/S1744309107001388.
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@article{osti_22360258,
title = {Crystallization and preliminary X-ray diffraction study of glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis},
author = {Katsumi, Ryota and Koga, Yuichi and You, Dong-Ju and Matsumura, Hiroyoshi and CREST and Takano, Kazufumi and CREST and Kanaya, Shigenori, E-mail: kanaya@mls.eng.osaka-u.ac.jp},
abstractNote = {Glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis was crystallized and preliminary crystallographic studies of the crystals were performed. Glycerol kinase from the hyperthermophilic archaeon Thermococcus kodakaraensis was crystallized and preliminary crystallographic studies of the crystals were performed. Crystals were grown at 293 K by the sitting-drop vapour-diffusion method. Native X-ray diffraction data were collected to 2.4 Å resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 Å. Assuming the presence of two molecules in the asymmetric unit, the V{sub M} value was 2.7 Å{sup 3} Da{sup −1} and the solvent content was 54.1%. The protein was also cocrystallized with substrates and diffraction data were collected to 2.7 Å resolution.},
doi = {10.1107/S1744309107001388},
journal = {Acta Crystallographica. Section F},
number = Pt 2,
volume = 63,
place = {United Kingdom},
year = {Thu Feb 01 00:00:00 EST 2007},
month = {Thu Feb 01 00:00:00 EST 2007}
}
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Journal Article:
DOI:  10.1107/S1744309107001388
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