ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage λ, was solved by multiwavelength anomalous diffraction (MAD) for a selenomethionine (SeMet) derivative of the protein at 1.8 Å resolution, using crystals in space group P21 [Yang et al. (2000), Nature Struct. Biol. 7, 230–237]. Subsequent analysis showed that the crystals of both the original protein and the SeMet derivative were pseudo-merohedrally twinned with a twinning fraction ∼ 0.36, owing to the near-identity of the a and c axes. An analysis of the crystal structure solution is presented and the utility of twinned crystals for solving the structure using MAD and of different phasing strategies is discussed; the results obtained with several software packages are compared.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444900007162
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