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Crystallization and preliminary x-ray diffraction analysis of the lumazine synthase from Brucella abortus.
J Struct Biol. 1998 Oct; 123(2):175-8.JS

Abstract

Lumazine synthase from Brucella abortus was overexpressed in Escherichia coli, refolded, and purified to apparent homogeneity. Crystals of lumazine synthase were grown by the hanging drop vapor diffusion method using polyethylene glycol 8000 or ammonium sulfate as precipitants. They belong to the trigonal space group P321 with cell parameters a = b = 132.00A, c = 167.25 A. A complete diffraction data set to 3.7 A resolution has been collected using synchrotron radiation. Preliminary analysis of the quaternary structure of this protein by means of a self-rotation function calculated with the diffraction data clearly indicates 532 symmetry compatible with the presence of an icosahedral lumazine synthase particle.

Authors+Show Affiliations

Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9843672

Citation

Goldbaum, F A., et al. "Crystallization and Preliminary X-ray Diffraction Analysis of the Lumazine Synthase From Brucella Abortus." Journal of Structural Biology, vol. 123, no. 2, 1998, pp. 175-8.
Goldbaum FA, Polikarpov I, Cauerhff AA, et al. Crystallization and preliminary x-ray diffraction analysis of the lumazine synthase from Brucella abortus. J Struct Biol. 1998;123(2):175-8.
Goldbaum, F. A., Polikarpov, I., Cauerhff, A. A., Velikovsky, C. A., Braden, B. C., & Poljak, R. J. (1998). Crystallization and preliminary x-ray diffraction analysis of the lumazine synthase from Brucella abortus. Journal of Structural Biology, 123(2), 175-8.
Goldbaum FA, et al. Crystallization and Preliminary X-ray Diffraction Analysis of the Lumazine Synthase From Brucella Abortus. J Struct Biol. 1998;123(2):175-8. PubMed PMID: 9843672.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary x-ray diffraction analysis of the lumazine synthase from Brucella abortus. AU - Goldbaum,F A, AU - Polikarpov,I, AU - Cauerhff,A A, AU - Velikovsky,C A, AU - Braden,B C, AU - Poljak,R J, PY - 1998/12/9/pubmed PY - 1998/12/9/medline PY - 1998/12/9/entrez SP - 175 EP - 8 JF - Journal of structural biology JO - J Struct Biol VL - 123 IS - 2 N2 - Lumazine synthase from Brucella abortus was overexpressed in Escherichia coli, refolded, and purified to apparent homogeneity. Crystals of lumazine synthase were grown by the hanging drop vapor diffusion method using polyethylene glycol 8000 or ammonium sulfate as precipitants. They belong to the trigonal space group P321 with cell parameters a = b = 132.00A, c = 167.25 A. A complete diffraction data set to 3.7 A resolution has been collected using synchrotron radiation. Preliminary analysis of the quaternary structure of this protein by means of a self-rotation function calculated with the diffraction data clearly indicates 532 symmetry compatible with the presence of an icosahedral lumazine synthase particle. SN - 1047-8477 UR - https://www.unboundmedicine.com/medline/citation/9843672/Crystallization_and_preliminary_x_ray_diffraction_analysis_of_the_lumazine_synthase_from_Brucella_abortus_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1047-8477(98)94022-9 DB - PRIME DP - Unbound Medicine ER -