2id8

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Revision as of 10:08, 21 November 2007

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spinqualitylabelsall models 2id8, resolution 1.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 CA, NO3, CL and 2DB 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

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