Comparison of phasing methods for sulfur-SAD using in-house chromium radiation : case studies for standard proteins and 69-kDa protein
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Phasing of the crystal structures of four standard proteins (lysozyme, trypsin, glucose isomerase, andthaumatin) and a novel 69-kDa protein from Thermus thermophilus, TT0570, was performed using the singlewavelengthanomalous diffraction of sulfur atoms intrinsically present within the native protein molecules. To utilizethe sulfur anomalous diffraction, the data sets were collected using the loop-less data collection method withchromium Kα X-rays of 2.29Å. Three phasing methods, MLPHARE, SHARP, and OASIS-2004, were tested incombination with the DM or SOLOMON density modification method. The results showed that the solvent contentsare still an important factor for phasing with the S-SAD method, even when longer wavelength Cr Kα radiation isused. Among the three procedures, the improved direct phasing of OASIS-2004 with its implemented fragmentfeedback to the direct-method probability calculation gave the best results in determining the initial phases. For allfive proteins, almost the entire models could be built automatically.
- International Union of Crystallographyの論文
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