Purification, crystallization, and preliminary X-ray diffraction analysis of the Tricorn protease hexamer from Thermoplasma acidophilum

Journal of Structural Biology

Volumn 134, Issue 1, 2001, Pages 83-87

  Bosch, Jürgen ^a   Tamura, Tomohiro ^b   Bourenkov, Gleb ^c   Baumeister, Wolfgang ^a   Essen, Lars Oliver ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY AIST   (Japan)

^c MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

Author keywords

Electron microscopy; Self compartmentalizing protease; Thermophile; Tricorn; X ray crystallography

Indexed keywords

CAPSID PROTEIN; PROTEINASE; RECOMBINANT ENZYME; SOLVENT;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ELECTRON MICROSCOPY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; IONIC STRENGTH; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; SYNCHROTRON RADIATION; THERMOPLASMA ACIDOPHILUM; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

MIRIDAE; THERMOPLASMA ACIDOPHILUM;

EID: 18744376560     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4360     Document Type: Article

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