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Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8.
J Mol Biol. 1993 Apr 05; 230(3):1086-8.JM

Abstract

The thermophile NADH oxidase from Thermus thermophilus, cloned and expressed in Escherichia coli, has been purified to homogeneity and crystallized. Three different crystal forms were found to be suitable for X-ray diffraction analysis. Crystals of the tetragonal form, grown in the presence of 25% polyethylene glycol 4000 and 0.25 M-NaCl at pH 6.6, were chosen for further analysis. These crystals belong to the space group P4(1)(3)2(1)2 with refined lattice constants of a = 94.8 A and c = 49.0 A, indicating a cell content of one monomer per asymmetric unit of the crystal. The crystals diffract to a resolution of 2.2 A.

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Authors+Show Affiliations

Erdmann H
GBF, Gesellschaft für Biotechnologische Forschung mbH, Braunschweig, Germany.
Hecht HJ
No affiliation info available
Park HJ
No affiliation info available
Sprinzl M
No affiliation info available
Schomburg D
No affiliation info available
Schmid RD
No affiliation info available

MeSH

Cloning, MolecularCrystallizationEscherichia coliMultienzyme ComplexesNADH, NADPH OxidoreductasesRecombinant ProteinsThermus thermophilusX-Ray Diffraction

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8478921

Citation

Erdmann, H, et al. "Crystallization and Preliminary X-ray Diffraction Studies of a NADH Oxidase From Thermus Thermophilus HB8." Journal of Molecular Biology, vol. 230, no. 3, 1993, pp. 1086-8.
Erdmann H, Hecht HJ, Park HJ, et al. Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8. J Mol Biol. 1993;230(3):1086-8.
Erdmann, H., Hecht, H. J., Park, H. J., Sprinzl, M., Schomburg, D., & Schmid, R. D. (1993). Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8. Journal of Molecular Biology, 230(3), 1086-8.
Erdmann H, et al. Crystallization and Preliminary X-ray Diffraction Studies of a NADH Oxidase From Thermus Thermophilus HB8. J Mol Biol. 1993 Apr 5;230(3):1086-8. PubMed PMID: 8478921.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction studies of a NADH oxidase from Thermus thermophilus HB8. AU - Erdmann,H, AU - Hecht,H J, AU - Park,H J, AU - Sprinzl,M, AU - Schomburg,D, AU - Schmid,R D, PY - 1993/4/5/pubmed PY - 1993/4/5/medline PY - 1993/4/5/entrez SP - 1086 EP - 8 JF - Journal of molecular biology JO - J Mol Biol VL - 230 IS - 3 N2 - The thermophile NADH oxidase from Thermus thermophilus, cloned and expressed in Escherichia coli, has been purified to homogeneity and crystallized. Three different crystal forms were found to be suitable for X-ray diffraction analysis. Crystals of the tetragonal form, grown in the presence of 25% polyethylene glycol 4000 and 0.25 M-NaCl at pH 6.6, were chosen for further analysis. These crystals belong to the space group P4(1)(3)2(1)2 with refined lattice constants of a = 94.8 A and c = 49.0 A, indicating a cell content of one monomer per asymmetric unit of the crystal. The crystals diffract to a resolution of 2.2 A. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8478921/Crystallization_and_preliminary_X_ray_diffraction_studies_of_a_NADH_oxidase_from_Thermus_thermophilus_HB8_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(83)71222-2 DB - PRIME DP - Unbound Medicine ER -