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Title: Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase

Abstract

T. maritima mannitol dehydrogenase has been crystallized in space group P2{sub 1}2{sub 1}2{sub 1} with a = 84.43, b = 120.61, c = 145.76 Å. The crystals diffracted to 3.3 Å resolution at the Canadian Light Source. Diffraction data have been collected from a crystal of Thermotoga maritima mannitol dehydrogenase at the Canadian Light Source. The crystal diffracted to 3.3 Å resolution and belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 83.43, b = 120.61, c = 145.76 Å. The structure is likely to be solved by molecular replacement.

Authors:
 [1]; ;  [2]; ;  [3];  [1]
  1. Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5 (Canada)
  2. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319 (United States)
  3. Canadian Macromolecular Facility, Canadian Light Source Inc., University of Saskatchewan, Saskatoon, Saskatchewan S7N 0X4 (Canada)
Publication Date:
OSTI Identifier:
22360315
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 4; Other Information: PMCID: PMC2330225; PMID: 17401214; PUBLISHER-ID: pu5179; OAI: oai:pubmedcentral.nih.gov:2330225; 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; LIGHT SOURCES; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Puttick, Jennifer, Vieille, Claire, Song, Seung H., Fodje, Michel N., Grochulski, Pawel, and Delbaere, Louis T. J., E-mail: louis.delbaere@usask.ca. Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107013097.
Puttick, Jennifer, Vieille, Claire, Song, Seung H., Fodje, Michel N., Grochulski, Pawel, & Delbaere, Louis T. J., E-mail: louis.delbaere@usask.ca. Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase. United Kingdom. doi:10.1107/S1744309107013097.
Puttick, Jennifer, Vieille, Claire, Song, Seung H., Fodje, Michel N., Grochulski, Pawel, and Delbaere, Louis T. J., E-mail: louis.delbaere@usask.ca. Sun . "Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase". United Kingdom. doi:10.1107/S1744309107013097.
@article{osti_22360315,
title = {Crystallization, preliminary X-ray diffraction and structure analysis of Thermotoga maritima mannitol dehydrogenase},
author = {Puttick, Jennifer and Vieille, Claire and Song, Seung H. and Fodje, Michel N. and Grochulski, Pawel and Delbaere, Louis T. J., E-mail: louis.delbaere@usask.ca},
abstractNote = {T. maritima mannitol dehydrogenase has been crystallized in space group P2{sub 1}2{sub 1}2{sub 1} with a = 84.43, b = 120.61, c = 145.76 Å. The crystals diffracted to 3.3 Å resolution at the Canadian Light Source. Diffraction data have been collected from a crystal of Thermotoga maritima mannitol dehydrogenase at the Canadian Light Source. The crystal diffracted to 3.3 Å resolution and belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 83.43, b = 120.61, c = 145.76 Å. The structure is likely to be solved by molecular replacement.},
doi = {10.1107/S1744309107013097},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}