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Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum.
Acta Crystallogr D Biol Crystallogr. 2004 Apr; 60(Pt 4):715-7.AC

Abstract

NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum was crystallized in the apo- and holoenzyme forms. Crystals were obtained using 2-propanol and polyethylene glycol MME 550 as precipitants for the apoenzyme and holoenzyme, respectively. The apoenzyme crystals belong to the trigonal space group P3(1)21 or its enantiomorph P3(2)21. The asymmetric unit contains three subunits; the values of the Matthews coefficient (VM) and the solvent content are 2.9 A3 Da-1 and 57%, respectively. A native data set was collected to a highest resolution limit of 4.0 A on an in-house X-ray source using a rotating-anode generator (overall Rsym of 12.3% and completeness of 97%). The holoenzyme crystals belong to the orthorhombic space group P2(1)2(1)2(1); the asymmetric unit contains one hexamer, giving a VM of 2.79 A3 Da-1 and a solvent content of 55%. Native and derivative data sets were collected. The crystals diffract to a maximum resolution of 2.8 A on the KEK-NW12 beamline at the Photon Factory and gave a data set with an overall Rsym of 7.9% and a completeness of 91%. Attempts are being made to solve the structure by the SIRAS method.

Authors+Show Affiliations

Bhuiya MW
Department of Biological Science and Technology, Faculty of Engineering,The University of Tokushima, 2-1 Minamijosanjima-cho, Tokushima 770-8506, Japan.
Sakuraba H
No affiliation info available
Yoneda K
No affiliation info available
Ohshima T
No affiliation info available
Imagawa T
No affiliation info available
Katunuma N
No affiliation info available
Tsuge H
No affiliation info available

MeSH

Archaeal ProteinsCloning, MolecularCrystallizationCrystallography, X-RayEnzyme StabilityGlutamate Dehydrogenase (NADP+)

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15039563

Citation

Bhuiya, Mohammad W., et al. "Crystallization and Preliminary X-ray Diffraction Analysis of the Hyperthermostable NAD-dependent Glutamate Dehydrogenase From Pyrobaculum Islandicum." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 4, 2004, pp. 715-7.
Bhuiya MW, Sakuraba H, Yoneda K, et al. Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):715-7.
Bhuiya, M. W., Sakuraba, H., Yoneda, K., Ohshima, T., Imagawa, T., Katunuma, N., & Tsuge, H. (2004). Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 4), 715-7.
Bhuiya MW, et al. Crystallization and Preliminary X-ray Diffraction Analysis of the Hyperthermostable NAD-dependent Glutamate Dehydrogenase From Pyrobaculum Islandicum. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):715-7. PubMed PMID: 15039563.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction analysis of the hyperthermostable NAD-dependent glutamate dehydrogenase from Pyrobaculum islandicum. AU - Bhuiya,Mohammad W, AU - Sakuraba,Haruhiko, AU - Yoneda,Kazunari, AU - Ohshima,Toshihisa, AU - Imagawa,Takahito, AU - Katunuma,Nobuhiko, AU - Tsuge,Hideaki, Y1 - 2004/03/23/ PY - 2003/10/20/received PY - 2004/01/24/accepted PY - 2004/3/25/pubmed PY - 2004/12/16/medline PY - 2004/3/25/entrez SP - 715 EP - 7 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 4 N2 - NAD-dependent glutamate dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum was crystallized in the apo- and holoenzyme forms. Crystals were obtained using 2-propanol and polyethylene glycol MME 550 as precipitants for the apoenzyme and holoenzyme, respectively. The apoenzyme crystals belong to the trigonal space group P3(1)21 or its enantiomorph P3(2)21. The asymmetric unit contains three subunits; the values of the Matthews coefficient (VM) and the solvent content are 2.9 A3 Da-1 and 57%, respectively. A native data set was collected to a highest resolution limit of 4.0 A on an in-house X-ray source using a rotating-anode generator (overall Rsym of 12.3% and completeness of 97%). The holoenzyme crystals belong to the orthorhombic space group P2(1)2(1)2(1); the asymmetric unit contains one hexamer, giving a VM of 2.79 A3 Da-1 and a solvent content of 55%. Native and derivative data sets were collected. The crystals diffract to a maximum resolution of 2.8 A on the KEK-NW12 beamline at the Photon Factory and gave a data set with an overall Rsym of 7.9% and a completeness of 91%. Attempts are being made to solve the structure by the SIRAS method. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15039563/Crystallization_and_preliminary_X_ray_diffraction_analysis_of_the_hyperthermostable_NAD_dependent_glutamate_dehydrogenase_from_Pyrobaculum_islandicum_ DB - PRIME DP - Unbound Medicine ER -