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Crystallization and preliminary X‐ray diffraction study of the green flavoenzyme 5‐Hydroxyvaleryl‐CoA dehydratase/dehydrogenase from Clostridium aminovalericum
Author(s) -
Eikmanns Ulrich,
Buta Christiane,
Buckel Wolfgang,
Pai Emil F.
Publication year - 1994
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/prot.340190310
Subject(s) - monoclinic crystal system , ammonium sulfate , polyethylene glycol , crystallization , crystallography , dehydratase , monomer , dehydrogenase , chemistry , resolution (logic) , crystal structure , polymer , enzyme , biochemistry , organic chemistry , artificial intelligence , computer science
Abstract The bifunctional flavoenzyme 5‐hydroxyvaleryl‐CoA dehydratase/ dehydrogenase has been crystallized from solutions containing ammonium sulfate (form I) or polyethylene glycol (form II) as precipitant. In both cases, the crystals grew in the monoclinic space group C2. The unit cell dimensions for form I crystals were determined as a = 162.8 Å, b = 71.8 Å, c = 83.5 Å, β = 109.1°. Corresponding values for form II crystals were a = 161.2 Å, b = 71.6 Å, c = 82.2 Å, β = 109.3°. In both cases most probably there are two monomers per asymmetric unit. The crystals diffract to about 2 Å resolution and are rather stable in the X‐ray beam. © 1994 Wiley‐Liss, Inc.