1rb4: Difference between revisions

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[[Image:1rb4.jpg|left|200px]]<br /><applet load="1rb4" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1rb4.jpg|left|200px]]<br /><applet load="1rb4" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1rb4, resolution 1.9Å" />

'''ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TETRAGONAL AUTOMATIC SOLUTION'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1RB4 OCA].

1RB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RB4 OCA].

==Reference==

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[[Category: peptide]]

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@@ Line 1: / Line 1: @@
-[[Image:1rb4.jpg|left|200px]]<br /><applet load="1rb4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rb4.jpg|left|200px]]<br /><applet load="1rb4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rb4, resolution 1.9&Aring;" />
 '''ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TETRAGONAL AUTOMATIC SOLUTION'''<br />
 ==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.
+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==
-RB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RB4 OCA].
+RB4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RB4 OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: peptide]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:25:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:59 2008''