Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli

The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. Crystals grew as orthorhombic plates with cell dimensions a = 58 A, b = 73 A, and c = 205 A. The asymmetric unit probably contains one B2 dimer of molecular weight 2 X 43...

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Bibliographic Details
Published in:The Journal of biological chemistry 1984-07, Vol.259 (14), p.9076-9077
Main Authors: Joelson, T, Uhlin, U, Eklund, H, Sjöberg, B M, Hahne, S, Karlsson, M
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Enzymes and enzyme inhibitors
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Macromolecular Substances
Oxidoreductases
Protein Conformation
Ribonucleotide Reductases - isolation & purification
X-Ray Diffraction
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Summary:The B2 subunit of ribonucleotide reductase from Escherichia coli has been crystallized from ammonium sulfate solutions at pH 6.0. Crystals grew as orthorhombic plates with cell dimensions a = 58 A, b = 73 A, and c = 205 A. The asymmetric unit probably contains one B2 dimer of molecular weight 2 X 43,000. The packing of molecules in the crystals is compatible with an elongated shape of the dimer. The crystals diffract to 2.5 A and are suitable for structural work.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)47266-8