Crystallization and preliminary X-ray analysis of IND, an enzyme with indole oxygenase activity from Chromobacterium violaceum

IND, a redox flavoprotein from Chromobacterium violaceum has been crystallized in the presence and absence of NADH. The crystals belong to the space group P41212 or its enantiomorph P43212 with a = 73.9 and c = 153.6 Å. There is one molecule per asymmetric unit and the crystals diffract beyond 2.1 Å...

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Published inActa crystallographica. Section D, Biological crystallography. Vol. 54; no. 4; pp. 657 - 658
Main Authors Cheah, E., MacPherson, K., Quiggin, D., Keese, P., Ollis, D. L.
Format Journal Article
LanguageEnglish
Published 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.07.1998
Subjects
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Chromobacterium - enzymology
Crystallization
Crystallography, X-Ray
Dioxygenases
Indoleamine-Pyrrole 2,3,-Dioxygenase
Oxygenases - chemistry
Oxygenases - isolation & purification
Protein Conformation
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - isolation & purification
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Summary:IND, a redox flavoprotein from Chromobacterium violaceum has been crystallized in the presence and absence of NADH. The crystals belong to the space group P41212 or its enantiomorph P43212 with a = 73.9 and c = 153.6 Å. There is one molecule per asymmetric unit and the crystals diffract beyond 2.1 Å resolution.
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ark:/67375/WNG-XGQVG37D-F
ArticleID:AYDGR0789
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444997018994