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 A. There is one molecule per asymmetric unit and the crystals diffract beyond 2.1 A resolution.
Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.
E
E
Cheah
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MacPherson
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D
Quiggin
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Keese
D L
DL
Ollis
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002861:Chromobacterium / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D049308:Dioxygenases; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D011993:Recombinant Fusion Proteins; D010105:Oxygenases; D049308:Dioxygenases