Thermostable xylanase from Thermoascus aurantiacus at ultrahigh resolution (0.89 Å) at 100 K and atomic resolution (1.11 Å) at 293 K refined anisotropically to small-molecule accuracy

Acta Crystallographica - Section D Biological Crystallography

Volumn 59, Issue 1, 2003, Pages 105-117

  Natesh, R ^a,b   Manikandan, K ^a   Bhanumoorthy, P ^a,c   Viswamitra, M A ^a   Ramakumar, S ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b University of Bath   (United Kingdom)

^c PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GLUTAMIC ACID; WATER; XYLAN 1,4 BETA XYLOSIDASE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ANISOTROPY; ARTICLE; ASCOMYCETES; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME STABILITY; ENZYMOLOGY; HYDROGEN BOND; METHODOLOGY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

ANISOTROPY; ARGININE; ASCOMYCOTA; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; GLUTAMIC ACID; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; WATER; XYLAN ENDO-1,3-BETA-XYLOSIDASE; XYLOSIDASES;

ASCOMYCOTA; BACTERIA (MICROORGANISMS); THERMOASCUS AURANTIACUS;

EID: 0037244052     PISSN: 09074449     EISSN: None     Source Type: Journal    
DOI: 10.1107/S0907444902020164     Document Type: Article

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