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Purification and crystallization of Pseudomonas aeruginosa chloramphenicol acetyltransferase
Author(s) -
Tian Yu,
Beaman Todd W.,
Roderick Steven L.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199706)28:2<298::aid-prot18>3.0.co;2-d
Subject(s) - chloramphenicol acetyltransferase , chloramphenicol , crystallization , pseudomonas aeruginosa , acetyltransferase , resolution (logic) , chemistry , ether , crystallography , microbiology and biotechnology , biology , antibiotics , biochemistry , bacteria , gene , genetics , organic chemistry , gene expression , promoter , artificial intelligence , computer science , acetylation
A chloramphenicol acetyltransferase from Pseudomonas aeruginosa genomic DNA has been overexpressed, refolded, purified, and crystallized. Crystals suitable for a three‐dimensional x‐ray structure determination were obtained from solutions of polyethyleneglycol methyl ether 2000 containing NiCl 2 at pH 8.5. These crystals belong to the cubic space group P4 1/3 32 (a = 154.8 Å) and diffract x‐rays to ≈3.2 Å resolution. Proteins 28:298–300, 1997. © 1997 Wiley‐Liss Inc.