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Crystallization and preliminary X-ray analysis of IND, an enzyme with indole oxygenase activity from Chromobacterium violaceum.
Cheah, E; MacPherson, K; Quiggin, D; Keese, P; Ollis, D L.
Acta Crystallogr D Biol Crystallogr ; 54(Pt 4): 657-8, 1998 Jul 01.
Article in English | MEDLINE | ID: mdl-9761866

ABSTRACT

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 A. There is one molecule per asymmetric unit and the crystals diffract beyond 2.1 A resolution.


Subject(s)
Bacterial Proteins/chemistry , Chromobacterium/enzymology , Dioxygenases , Oxygenases/chemistry , Bacterial Proteins/isolation & purification , Crystallization , Crystallography, X-Ray , Indoleamine-Pyrrole 2,3,-Dioxygenase , Oxygenases/isolation & purification , Protein Conformation , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/isolation & purification
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