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2id8
From Proteopedia
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Crystal structure of Proteinase K
Overview
X-ray single-wavelength anomalous diffraction (SAD) data from a crystal of proteinase K were collected using synchrotron radiation of 0.98 A wavelength at SER-CAT 22-ID beamline, Advanced Photon Source, Argonne National Laboratory. At this wavelength, the expected Bijvoet ratio resulting from the presence of one calcium, one chloride and ten S atoms in the 279-residue protein is extremely small at approximately 0.46%. The direct-methods program SHELXD located 11 anomalous sites using data truncated to 2 A resolution. SHELXE was used to produce an easily interpretable electron-density map. This study shows that an accurate beamline and a good-quality crystal provide the possibility of successfully using a very weak anomalous signal of sulfur measured at a short wavelength for phasing a protein structure, even if a small degree of radiation damage is present.
About this Structure
2ID8 is a Single protein structure of sequence from Engyodontium album with , , and as ligands. Active as Peptidase K, with EC number 3.4.21.64 Full crystallographic information is available from OCA.
Reference
What can be done with a good crystal and an accurate beamline?, Wang J, Dauter M, Dauter Z, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1475-83. Epub 2006, Nov 23. PMID:17139083
Page seeded by OCA on Thu Feb 21 17:51:27 2008
Categories: Engyodontium album | Peptidase K | Single protein | Dauter, M. | Dauter, Z. | Wang, J. | 2DB | CA | CL | NO3 | Proteinase
