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Title: Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8

Abstract

The glucose dehydrogenase (GDH) protein from T. thermophilus HB8 was cloned, expressed, purified and crystallized. GDH crystals belong to space group P2{sub 1} and diffract to 1.9 Å resolution. Thermus thermophilus is an aerobic chemoorganotroph that has been found to grow anaerobically in the presence of nitrate. Crystals of glucose dehydrogenase (GDH) from T. thermophilus HB8 belong to space group P2{sub 1}, with unit-cell parameters a = 36.90, b = 132.96, c = 60.78 Å, β = 97.2°. Preliminary studies and molecular-replacement calculations reveal that the asymmetric unit contains two monomers.

Authors:
;  [1]; ; ;  [2];  [2];  [3];  [2];  [4];  [2];  [3];  [2];  [2];  [3];  [2];  [3];  [2];  [1];  [5];  [2] more »;  [3];  [3];  [6] « less
  1. Bioinformatics Centre (Centre of Excellence in Structural Biology and Biocomputing), Indian Institute of Science, Bangalore 560 012 (India)
  2. RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148 (Japan)
  3. (Japan)
  4. Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo (Japan)
  5. (India)
  6. (Centre of Excellence in Structural Biology and Biocomputing), Indian Institute of Science, Bangalore 560 012 (India)
Publication Date:
OSTI Identifier:
22360320
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2334996; PMID: 17565193; PUBLISHER-ID: en5221; OAI: oai:pubmedcentral.nih.gov:2334996; 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; CRYSTALS; GLUCOSE; MONOMERS; RESOLUTION; SPACE GROUPS

Citation Formats

Kanaujia, Shankar Prasad, Ranjani, Chellamuthu Vasuki, Jeyakanthan, Jeyaraman, Nishida, Masami, Kitamura, Yoshiaki, Baba, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Ebihara, Akio, Shimizu, Nobutaka, Nakagawa, Noriko, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Shinkai, Akeo, Yamamoto, Masaki, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Kuramitsu, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Shiro, Yoshitsugu, Sekar, Kanagaraj, E-mail: sekar@physics.iisc.ernet.in, Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012, Yokoyama, Shigeyuki, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, and Bioinformatics Centre. Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107014819.
Kanaujia, Shankar Prasad, Ranjani, Chellamuthu Vasuki, Jeyakanthan, Jeyaraman, Nishida, Masami, Kitamura, Yoshiaki, Baba, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Ebihara, Akio, Shimizu, Nobutaka, Nakagawa, Noriko, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Shinkai, Akeo, Yamamoto, Masaki, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Kuramitsu, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Shiro, Yoshitsugu, Sekar, Kanagaraj, E-mail: sekar@physics.iisc.ernet.in, Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012, Yokoyama, Shigeyuki, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, & Bioinformatics Centre. Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8. United Kingdom. doi:10.1107/S1744309107014819.
Kanaujia, Shankar Prasad, Ranjani, Chellamuthu Vasuki, Jeyakanthan, Jeyaraman, Nishida, Masami, Kitamura, Yoshiaki, Baba, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Ebihara, Akio, Shimizu, Nobutaka, Nakagawa, Noriko, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Shinkai, Akeo, Yamamoto, Masaki, Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo, Kuramitsu, Seiki, Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Shiro, Yoshitsugu, Sekar, Kanagaraj, E-mail: sekar@physics.iisc.ernet.in, Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012, Yokoyama, Shigeyuki, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, and Bioinformatics Centre. Tue . "Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8". United Kingdom. doi:10.1107/S1744309107014819.
@article{osti_22360320,
title = {Preliminary X-ray crystallographic study of glucose dehydrogenase from Thermus thermophilus HB8},
author = {Kanaujia, Shankar Prasad and Ranjani, Chellamuthu Vasuki and Jeyakanthan, Jeyaraman and Nishida, Masami and Kitamura, Yoshiaki and Baba, Seiki and Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 and Ebihara, Akio and Shimizu, Nobutaka and Nakagawa, Noriko and Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo and Shinkai, Akeo and Yamamoto, Masaki and Japan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5198, Hyogo and Kuramitsu, Seiki and Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 and Shiro, Yoshitsugu and Sekar, Kanagaraj, E-mail: sekar@physics.iisc.ernet.in and Supercomputer Education and Research Centre, Indian Institute of Science, Bangalore 560 012 and Yokoyama, Shigeyuki and RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045 and Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033 and Bioinformatics Centre},
abstractNote = {The glucose dehydrogenase (GDH) protein from T. thermophilus HB8 was cloned, expressed, purified and crystallized. GDH crystals belong to space group P2{sub 1} and diffract to 1.9 Å resolution. Thermus thermophilus is an aerobic chemoorganotroph that has been found to grow anaerobically in the presence of nitrate. Crystals of glucose dehydrogenase (GDH) from T. thermophilus HB8 belong to space group P2{sub 1}, with unit-cell parameters a = 36.90, b = 132.96, c = 60.78 Å, β = 97.2°. Preliminary studies and molecular-replacement calculations reveal that the asymmetric unit contains two monomers.},
doi = {10.1107/S1744309107014819},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}