A quasi-Laue neutron crystallographic study of D-xylose isomerase

European Biophysics Journal

Volumn 35, Issue 7, 2006, Pages 601-609

  Meilleur, Flora ^a   Snell, Edward H ^b   Van Der Woerd, Mark J ^c   Judge, Russell A ^d   Myles, Dean A A ^e  

^a INSTITUT LAUE LANGEVIN   (France)

^b HAUPTMAN WOODWARD MEDICAL RESEARCH INSTITUTE   (United States)

^c BAE SYSTEMS   (United States)

^d ABBOTT LABORATORIES   (United States)

^e OAK RIDGE NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; DEUTERIUM; GLUTAMIC ACID; GLUTAMINE; HISTIDINE; HYDROGEN; TRYPTOPHAN; WATER; XYLOSE ISOMERASE;

ARTICLE; CATALYSIS; CONFORMATION; CRYSTAL; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME STRUCTURE; ISOMERIZATION; MACROMOLECULE; NEUTRON DIFFRACTION; NEUTRON SCATTERING; PROTON TRANSPORT; RING OPENING; ROOM TEMPERATURE; STREPTOMYCES; X RAY CRYSTALLOGRAPHY;

ALDOSE-KETOSE ISOMERASES; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; HYDROGEN; MODELS, CHEMICAL; NEUTRON DIFFRACTION; NEUTRONS; PROTEIN BINDING; STREPTOMYCES; XYLOSE;

STREPTOMYCES RUBIGINOSUS;

EID: 33748541458     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-006-0066-6     Document Type: Article

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