Crystallization of the Bacillus subtilis histidine-containing phosphocarrier protein HPr and of some of its site-directed mutants.
The histidine-containing phosphocarrier protein (HPr) from Bacillus subtilis has been crystallized. Two of the site-directed mutants aimed at probing function produce crystals suitable for X-ray studies. The mutant in which His15 is substituted by an alanyl residue crystallizes from ammonium sulfate solution in space group P3(1)21 or P3(2)21, with unit cell dimensions: a = b = 47.3 A; c = 61.5 A. These crystals diffract to at least 1.8 A resolution. The mutant in which Ser46 is substituted by an aspartyl residue crystallizes from polyethylene glycol 4000 solution in space group P2(1), with unit cell dimensions: a = 49.4 A; b = 25.6 A; c = 60.3 A; beta = 109 degrees. These crystals diffract to at least 2.0 A resolution.
Kapadia
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Center for Advanced Research in Biotechnology, University of Maryland, Rockville 20850.
Reizer
J
J
Sutrina
S L
SL
Saier
M H
MH
Reddy
P
P
Herzberg
O
O
D001412:Bacillus subtilis; D001426:Bacterial Proteins; D003460:Crystallization; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D011092:Polyethylene Glycols; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D011092:Polyethylene Glycols; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr