Expression, purification and crystallization of enterococcus faecium streptogramin A acetyltransferase.
The streptogramin A acetyltransferase from Enterococcus faecium (SWISS-PROT P50870) has been overexpressed in Escherichia coli, purified and crystallized. Crystallization conditions were screened using the hanging-drop vapor-diffusion method and resulted in two distinct crystal forms. Form I crystals diffract to 2.5 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.6, b = 102.6, c = 107.5 A. Form II crystals diffract to 2.7 A and belong to space group F222, with unit-cell parameters a = 185.8, b = 185.8, c = 186.5 A. Rotation-function and packing analyses for both crystal forms indicate that the asymmetric unit may contain one and two copies of the trimeric enzyme for crystal forms I and II, respectively.
Sugantino
M
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Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Roderick
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SL
D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D016984:Enterococcus faecium / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D000123:Acetyltransferases; C084756:streptogramin A acetyltransferase, Enterococcus faecium