Crystallization and preliminary X-ray diffraction analysis of the chloramphenicol acetyltransferase from Tn2424.
Crystals of chloramphenicol acetyltransferase B2, an enzyme encoded by the transposon Tn2424 from Escherichia coli, have been obtained utilizing polyethylene glycol as a precipitant. The enzyme inactivates the antibiotic chloramphenicol and is a member of the xenobiotic acetyltransferase family. Two crystal forms were obtained and complete data sets have been collected at a synchrotron source: form I, which diffracted to 3.2 A, and form II, grown in the presence of NiCl(2), for which crystals of the apoenzyme and of the enzyme-chloramphenicol complex have been obtained. For the form II crystals, complete data sets have been collected at 2.7 and 3.2 A resolution, respectively. The space group of the above two crystal forms is P2(1)3, with unit-cell parameter a = 130 A.
Zhou
M
M
Molecular Endocrinology and Oncology Laboratory, CHUL Research Center and Laval University, Quebec, Canada.
Lu
M L
ML
Qiu
W
W
Campbell
R L
RL
Nahoum
V
V
Lapointe
J
J
Roy
P H
PH
Lin
S X
SX
D001051:Apoenzymes / Q000737:chemistry / Q000302:isolation & purification; D015500:Chloramphenicol O-Acetyltransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D004251:DNA Transposable Elements; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D011092:Polyethylene Glycols; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
D001051:Apoenzymes; D004251:DNA Transposable Elements; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D015500:Chloramphenicol O-Acetyltransferase