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

doi:10.1107/S1744309107013097

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

Full Record
Other Related Research

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:

Puttick, Jennifer ^[1]; Vieille, Claire; Song, Seung H. ^[2]; Fodje, Michel N.; Grochulski, Pawel ^[3]; Delbaere, Louis T. J., E-mail: louis.delbaere@usask.ca ^[1]

Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5 (Canada)
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824-1319 (United States)
Canadian Macromolecular Facility, Canadian Light Source Inc., University of Saskatchewan, Saskatoon, Saskatchewan S7N 0X4 (Canada)

Publication Date:: Sun Apr 01 00:00:00 EDT 2007

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.

Copy to clipboard


                    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.

Copy to clipboard


                    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.

Copy to clipboard


                    
@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}

}

Copy to clipboard

Journal Article:

DOI: 10.1107/S1744309107013097

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Crystallization and preliminary X-ray analysis of cytosolic α-mannosidase from Thermotoga maritima

Journal Article Nakajima, Masahiro ; Fushinobu, Shinya, E-mail: asfushi@mail.ecc.u-tokyo.ac.jp ; Imamura, Hiromi ; ... - Acta Crystallographica. Section F

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.
DOI: 10.1107/S1744309105042508
Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritima

Journal Article Barbey, Carole, E-mail: carole.barbey@smbh.univ-paris13.fr ; Rouhier, Nicolas ; Haouz, Ahmed ; ... - Acta Crystallographica. Section F

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 »« less
DOI: 10.1107/S1744309107064391
Crystallization and preliminary X-ray crystallographic characterization of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima

Journal Article Cicmil, Nenad, E-mail: cicmil@uiuc.edu - Acta Crystallographica. Section F

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 »« less
DOI: 10.1107/S1744309108003825
Crystallization and preliminary X-ray diffraction analysis of a lectin from Canavalia maritima seeds

Journal Article Almeida Gadelha, Carlos Alberto de ; Moreno, Frederico Bruno Mendes Batista ; Santi-Gadelha, Tatiane ; ... - Acta Crystallographica. Section F

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 »« less
DOI: 10.1107/S1744309104029197
Crystallization and preliminary X-ray diffraction analysis of the arginine repressor of the hyperthermophile Thermotoga neapolitana

Journal Article Massant, Jan, E-mail: jan.massant@vub.ac.be ; Peeters, Eveline ; Charlier, Daniel ; ... - Acta Crystallographica. Section F

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 »« less
DOI: 10.1107/S1744309105039618

Similar Records