期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 62, 期 -, 页码 1031-1033出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309106036700
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Pyrrolysyl-tRNA synthetase (PylRS) from Methanosarcina mazei was over-expressed in an N-terminally truncated form PylRS(c270) in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. The native PylRS(c270) crystals in complex with an ATP analogue belonged to space group P6(4), with unit-cell parameters a = b = 104.88, c = 70.43 angstrom, alpha = beta = 90, gamma = 120 degrees, and diffracted to 1.9 angstrom resolution. The asymmetric unit contains one molecule of PylRS(c270). Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.
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