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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}
}
  • Cytosolic class II α-mannosidase from T. maritima (TM1851), a family 38 glycoside hydrolase, was crystallized. A diffraction data set was collected to 2.9 Å resolution. Class II α-mannosidase cleaves off α-1,2-, α-1,3- and α-1,6-mannose residues. In this paper, the crystallization and preliminary X-ray analysis of cytosolic class II α-mannosidase from Thermotoga maritima (TM1851), a family 38 glycoside hydrolase, is described. The crystal of recombinant TM1851 belongs to the C-centred monoclinic space group C2, with unit-cell parameters a = 244.7, b = 87.4, c = 166.6 Å, β = 124.7°. X-ray diffraction data were collected to a resolution of 2.9 Å.
  • Crystals of the peroxiredoxin domain of a larger natural hybrid protein from T. maritima were obtained which diffracted to 2.9 Å resolution on a synchrotron source. Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced and purified from Escherichia coli cells. The recombinant Prx domain, which is homologous to bacterial Prx BCP and plant Prx Q, folds properly into a stable protein that possesses biological activity. The recombinant protein was crystallized and synchrotron data were collected to 2.9more » Å resolution. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 176.67, c = 141.20 Å.« less
  • T. maritima TrmFO was overexpressed, purified and crystallized. A diffraction data set was collected to a resolution of 2.6 Å. TrmFO, previously classified as GID, is a methyltransferase that catalyzes the formation of 5-methyluridine or ribothymidine (T) at position 54 in tRNA in some Gram-positive bacteria. To date, TrmFO is the only characterized tRNA methyltransferase that does not use S-adenosylmethionine as the methyl-group donor. Instead, the donor of the methyl group is N{sup 5},N{sup 10}-methylenetetrahydrofolate. The crystallization and preliminary X-ray crystallographic studies of TrmFO are reported here. The recombinant protein, cloned from Thermotoga maritima genomic DNA, was overproduced in Esherichiamore » coli and crystallized in 25%(v/v) PEG 4000, 100 mM NaCl and sodium citrate buffer pH 5.0 at 291 K using the hanging-drop vapor-diffusion method. The plate-shaped crystals diffracted to 2.6 Å and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 79.94, b = 92.46, c = 127.20 Å.« less
  • A lectin from C. maritima was crystallized using the vapour-diffusion method and crystals diffracted to 2.1 Å resolution. A molecular-replacement search found a solution with a correlation coefficient of 69.2% and an R factor of 42.5%, refinement is in progress. A lectin from Canavalia maritima seeds (ConM) was purified and submitted to crystallization experiments. The best crystals were obtained using the vapour-diffusion method at a constant temperature of 293 K and grew in 7 d. A complete structural data set was collected to 2.1 Å resolution using a synchrotron-radiation source. The ConM crystal belongs to the orthorhombic space group P2{submore » 1}2{sub 1}2, with unit-cell parameters a = 67.15, b = 70.90, c = 97.37 Å. A molecular-replacement search found a solution with a correlation coefficient of 69.2% and an R factor of 42.5%. Crystallographic refinement is under way.« less
  • The arginine repressor of the hyperthermophile T. neapolitana was crystallized with and without its corepressor arginine. Both crystals diffracted to high resolution and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with similar unit-cell parameters. The arginine repressor of Thermotoga neapolitana (ArgRTnp) is a member of the family of multifunctional bacterial arginine repressors involved in the regulation of arginine metabolism. This hyperthermophilic repressor shows unique DNA-binding features that distinguish it from its homologues. ArgRTnp exists as a homotrimeric protein that assembles into hexamers at higher protein concentrations and/or in the presence of arginine. ArgRTnp was crystallized with andmore » without its corepressor arginine using the hanging-drop vapour-diffusion method. Crystals of the aporepressor diffracted to a resolution of 2.1 Å and belong to the orthorhombic P2{sub 1}2{sub 1}2{sub 1} space group, with unit-cell parameters a = 117.73, b = 134.15, c = 139.31 Å. Crystals of the repressor in the presence of its corepressor arginine diffracted to a resolution of 2.4 Å and belong to the same space group, with similar unit-cell parameters.« less