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Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum.
J Struct Biol. 2001 Apr; 134(1):83-7.JS

Abstract

Tricorn protease from Thermoplasma acidophilum is a hexameric enzyme; in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa. Recombinant Tricorn protease was purified as an enzymatically active hexamer of 0.72 MDa that formed crystals of octahedral morphology under low-ionic-strength conditions. These crystals belong to space group C2 with unit cell dimensions a = 307.5 A, b = 163.2 A, c = 220.9 A, beta = 105.5 degrees and diffract to 2.2-A resolution using high-brilliance synchrotron radiation. Based on analysis of the self-rotation function and the presence of a pseudo-origin peak in the native Patterson map, a packing model was derived for the complex, comprising 1.5 hexamers per asymmetric unit with a solvent content of 43%. Due to the ninefold noncrystallographic symmetry the Tricorn crystals represent an interesting case for phasing X-ray crystallographic data by electron microscopic phase information.

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Authors+Show Affiliations

Bosch J
Max-Planck-Institute of Biochemistry, Am Klopferspitz 18a, Martinsried bei München, D-82152, Germany.
Tamura T
No affiliation info available
Bourenkov G
No affiliation info available
Baumeister W
No affiliation info available
Essen LO
No affiliation info available

MeSH

Archaeal ProteinsCrystallizationEndopeptidasesMolecular ConformationThermoplasmaX-Ray Diffraction

Pub Type(s)

Journal Article

Language

eng

PubMed ID

11469880

Citation

Bosch, J, et al. "Purification, Crystallization, and Preliminary X-ray Diffraction Analysis of the Tricorn Protease Hexamer From Thermoplasma Acidophilum." Journal of Structural Biology, vol. 134, no. 1, 2001, pp. 83-7.
Bosch J, Tamura T, Bourenkov G, et al. Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum. J Struct Biol. 2001;134(1):83-7.
Bosch, J., Tamura, T., Bourenkov, G., Baumeister, W., & Essen, L. O. (2001). Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum. Journal of Structural Biology, 134(1), 83-7.
Bosch J, et al. Purification, Crystallization, and Preliminary X-ray Diffraction Analysis of the Tricorn Protease Hexamer From Thermoplasma Acidophilum. J Struct Biol. 2001;134(1):83-7. PubMed PMID: 11469880.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum. AU - Bosch,J, AU - Tamura,T, AU - Bourenkov,G, AU - Baumeister,W, AU - Essen,L O, PY - 2001/7/27/pubmed PY - 2002/1/29/medline PY - 2001/7/27/entrez SP - 83 EP - 7 JF - Journal of structural biology JO - J Struct Biol VL - 134 IS - 1 N2 - Tricorn protease from Thermoplasma acidophilum is a hexameric enzyme; in vivo the hexamers assemble further to form large icosahedral capsids of 14.6 MDa. Recombinant Tricorn protease was purified as an enzymatically active hexamer of 0.72 MDa that formed crystals of octahedral morphology under low-ionic-strength conditions. These crystals belong to space group C2 with unit cell dimensions a = 307.5 A, b = 163.2 A, c = 220.9 A, beta = 105.5 degrees and diffract to 2.2-A resolution using high-brilliance synchrotron radiation. Based on analysis of the self-rotation function and the presence of a pseudo-origin peak in the native Patterson map, a packing model was derived for the complex, comprising 1.5 hexamers per asymmetric unit with a solvent content of 43%. Due to the ninefold noncrystallographic symmetry the Tricorn crystals represent an interesting case for phasing X-ray crystallographic data by electron microscopic phase information. SN - 1047-8477 UR - https://www.unboundmedicine.com/medline/citation/11469880/Purification_crystallization_and_preliminary_X_ray_diffraction_analysis_of_the_Tricorn_protease_hexamer_from_Thermoplasma_acidophilum_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1047-8477(01)94360-6 DB - PRIME DP - Unbound Medicine ER -