1rb4
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(New page: 200px<br /><applet load="1rb4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rb4, resolution 1.9Å" /> '''ANTIPARALLEL TRIMER O...)
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Revision as of 23:18, 20 November 2007
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ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TETRAGONAL AUTOMATIC SOLUTION
Overview
Efficient determination of protein crystal structures requires automated, x-ray data analysis. Here, we describe the expert system ELVES and its use, to determine automatically the structure of a 12-kDa protein., Multiwavelength anomalous diffraction analysis of a selenomethionyl, derivative was used to image the Asn-16-Ala variant of the GCN4 leucine, zipper. In contrast to the parallel, dimeric coiled coil formed by the WT, sequence, the mutant unexpectedly formed an antiparallel trimer. This, structural switch reveals how avoidance of core cavities at a single site, can select the native fold of a protein. All structure calculations, including indexing, data processing, locating heavy atoms, phasing by, multiwavelength anomalous diffraction, model building, and refinement, were completed without human intervention. The results demonstrate the, feasibility of automated methods for determining high-resolution, x-ray, crystal structures of proteins.
About this Structure
1RB4 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Automated protein crystal structure determination using ELVES., Holton J, Alber T, Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1537-42. Epub 2004 Jan 29. PMID:14752198
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