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Title: Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus

Abstract

A GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus has been crystallized. Combined with biochemical analyses, it is expected that the structure of this protein will give insight in the function of a relatively unknown subfamily of the GTPase superfamily. A predicted GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus, termed SsGBP, has been cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion technique in the presence of 0.05 M cadmium sulfate and 0.8 M sodium acetate pH 7.5. A single-wavelength anomalous dispersion data set was collected to a maximum resolution of 2.0 Å using a single cadmium-incorporated crystal. The crystal form belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with approximate unit-cell parameters a = 65.0, b = 72.6, c = 95.9 Å and with a monomer in the asymmetric unit.

Authors:
;  [1];  [2];  [1];  [3];  [1];  [3];  [1]
  1. Laboratory of Microbiology, Department of Agrotechnology and Food Sciences, Wageningen University, Hesselink van Suchtelenweg 4, 6703 CT Wageningen (Netherlands)
  2. (China)
  3. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101 (China)
Publication Date:
OSTI Identifier:
22360274
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 3; Other Information: PMCID: PMC2330175; PMID: 17329823; PUBLISHER-ID: bw5186; OAI: oai:pubmedcentral.nih.gov:2330175; 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; ACETATES; CADMIUM; CRYSTALLIZATION; CRYSTALS; DIFFUSION; DISPERSIONS; ESCHERICHIA COLI; MONOMERS; PROTEINS; RESOLUTION; SODIUM; SPACE GROUPS; WAVELENGTHS

Citation Formats

Wu, Hao, Sun, Lei, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, Brouns, Stan J. J., Fu, Sheng, Akerboom, Jasper, Li, Xuemei, E-mail: lixm@sun5.ibp.ac.cn, and Oost, John van der, E-mail: lixm@sun5.ibp.ac.cn. Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107008500.
Wu, Hao, Sun, Lei, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, Brouns, Stan J. J., Fu, Sheng, Akerboom, Jasper, Li, Xuemei, E-mail: lixm@sun5.ibp.ac.cn, & Oost, John van der, E-mail: lixm@sun5.ibp.ac.cn. Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus. United Kingdom. doi:10.1107/S1744309107008500.
Wu, Hao, Sun, Lei, National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, Brouns, Stan J. J., Fu, Sheng, Akerboom, Jasper, Li, Xuemei, E-mail: lixm@sun5.ibp.ac.cn, and Oost, John van der, E-mail: lixm@sun5.ibp.ac.cn. Thu . "Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus". United Kingdom. doi:10.1107/S1744309107008500.
@article{osti_22360274,
title = {Purification, crystallization and preliminary crystallographic analysis of a GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus},
author = {Wu, Hao and Sun, Lei and National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101 and Brouns, Stan J. J. and Fu, Sheng and Akerboom, Jasper and Li, Xuemei, E-mail: lixm@sun5.ibp.ac.cn and Oost, John van der, E-mail: lixm@sun5.ibp.ac.cn},
abstractNote = {A GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus has been crystallized. Combined with biochemical analyses, it is expected that the structure of this protein will give insight in the function of a relatively unknown subfamily of the GTPase superfamily. A predicted GTP-binding protein from the hyperthermophilic archaeon Sulfolobus solfataricus, termed SsGBP, has been cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the hanging-drop vapour-diffusion technique in the presence of 0.05 M cadmium sulfate and 0.8 M sodium acetate pH 7.5. A single-wavelength anomalous dispersion data set was collected to a maximum resolution of 2.0 Å using a single cadmium-incorporated crystal. The crystal form belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with approximate unit-cell parameters a = 65.0, b = 72.6, c = 95.9 Å and with a monomer in the asymmetric unit.},
doi = {10.1107/S1744309107008500},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 63,
place = {United Kingdom},
year = {Thu Mar 01 00:00:00 EST 2007},
month = {Thu Mar 01 00:00:00 EST 2007}
}