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Preparation and crystallization of a cross‐linked complex of bovine adrenodoxin and adrenodoxin reductase
Author(s) -
Lapko Anna,
Müller Alexander,
Heese Olaf,
Ruckpaul Klaus,
Heinemann Udo
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199706)28:2<289::aid-prot16>3.0.co;2-e
Subject(s) - adrenodoxin , chemistry , crystallization , crystallography , stereochemistry , biochemistry , enzyme , organic chemistry , cytochrome
Bovine adrenodoxin was cross‐linked to adrenodoxin reductase with 1‐ethyl‐3‐(3‐dimethyl‐aminopropyl) carbodiimide. Mass spectrometry showed the reaction product to be a 1:1 complex of the two proteins with M r = 64,790 ± 50. The cross‐linked complex showed cytochrome c reductase activity and could be crystallized by hanging‐drop vapor diffusion. Crystals of the adrenodoxin‐adrenodoxin reductase complex are hexagonal, space group P6 1 22 or P6 5 22, with a = 93.26 Å and c = 612.20 Å and diffract to 2.9 Å resolution at 100 K. Assuming two cross‐linked complexes per asymmetric unit yields a reasonable V M of 2.97 Å 3 /Da. Proteins 28:289–292, 1997. © 1997 Wiley‐Liss Inc.