期刊
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷 63, 期 -, 页码 1069-1074出版社
BLACKWELL PUBLISHING
DOI: 10.1107/S0907444907042230
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资金
- ICREA Funding Source: Custom
NovP is an S-adenosyl-l-methionine-dependent O-methyl-transferase from Streptomyces spheroides ( subunit MW = 29 967 Da). Recombinant N-terminally His-tagged NovP crystallizes in space group P2, with approximate unit-cell parameters a = 51.81, b = 46.04, c = 61.22 angstrom, beta = 105.0 degrees, giving a solvent content of 44% for a single copy of the His-tagged protomer per asymmetric unit. Native synchrotron data to a resolution of 1.35 angstrom were combined with three other native data sets collected at lower resolution ( both in-house and at the synchrotron) for the sake of completeness and better scaling. Data to 2.45 angstrom resolution were subsequently recorded in-house from a single mercury derivative. Three partial mercury sites could be located with SHELXD, but the resulting phases had a mean error of about 81 degrees and in our hands did not yield an interpretable map using standard automated software. Nevertheless, the structure of NovP could be solved by first tracing a small part of the structure by hand and then extrapolating within and beyond the experimental resolution limit using the 'free lunch algorithm' in SHELXE. The resulting phases have a mean phase error of 17 degrees relative to a refined model.
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