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Crystallization and preliminary X-ray crystallographic data of a histidine-binding protein from Escherichia coli.

作者信息

Trakhanov S D, Yusifov E F

机构信息

Institute of Crystallography, Academy of Sciences of the USSR, Moscow.

出版信息

J Mol Biol. 1989 Jun 20;207(4):847-9. doi: 10.1016/0022-2836(89)90253-2.

DOI:10.1016/0022-2836(89)90253-2
PMID:2668541
Abstract

Histidine-binding protein, purified from periplasmic space of Escherichia coli K12, has been crystallized in a form suitable for X-ray analysis. Crystals of average size 0.3 mm x 0.15 mm x 0.15 mm have been grown by the hanging-drop method, with ammonium sulfate as precipitant. The space group if I4(1)22, with the unit cell dimensions a = b = 119.1 A; c = 151.8 A; Vm = 2.7 A3/dalton. There appear to be two protein subunits of molecular weight 25,000 each in the asymmetric unit.

摘要

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