AI Article Synopsis
- The enzyme chloramphenicol acetyltransferase B2, sourced from E. coli’s Tn2424 transposon, has been crystallized using polyethylene glycol as a precipitating agent.
- Two crystal forms of the enzyme were produced, with differing diffraction capabilities: form I at 3.2 Å and form II at 2.7 Å and 3.2 Å, with the latter developed in the presence of NiCl(2).
- Both forms belong to the same space group, P21(3), and have a unit-cell parameter of a = 130 Å.
Article Abstract
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.
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