Sub-ångström-resolution crystallography reveals physical distortions that enhance reactivity of a covalent enzymatic intermediate

Nature Chemistry

Volumn 5, Issue 9, 2013, Pages 762-767

  Lüdtke, Stefan ^a   Neumann, Piotr ^b   Erixon, Karl M ^c   Leeper, Finian ^c   Kluger, Ronald ^d   Ficner, Ralf ^b   Tittmann, Kai ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b UNIVERSITY OF GÖTTINGEN   (Germany)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^d UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

PENTOSE PHOSPHATE; TRANSKETOLASE; XYLULOSE 5 PHOSPHATE; XYLULOSE-5-PHOSPHATE;

ARTICLE; BINDING SITE; BIOCATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BINDING SITES; BIOCATALYSIS; CRYSTALLOGRAPHY, X-RAY; HUMANS; PENTOSEPHOSPHATES; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY; TRANSKETOLASE;

EID: 84883156844     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1728     Document Type: Article

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