2d6b: Difference between revisions

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New page: left|200px<br /><applet load="2d6b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d6b, resolution 1.25Å" /> '''Novel Bromate Specie...
 
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[[Image:2d6b.gif|left|200px]]<br /><applet load="2d6b" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2d6b.gif|left|200px]]<br /><applet load="2d6b" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2d6b, resolution 1.25&Aring;" />
caption="2d6b, resolution 1.25&Aring;" />
'''Novel Bromate Species trapped within a Protein Crystal'''<br />
'''Novel Bromate Species trapped within a Protein Crystal'''<br />


==Overview==
==Overview==
Only a few protein-oxoanion crystal complexes have been described to date., Here, the structure of a protein soaked in a bromate solution has been, determined to a resolution of 1.25 A and refined to final overall, R/R(free) values of 18.04/21.3 (isotropic) and 11.25/14.67 (anisotropic)., In contrast to the single-model approach, refinement of an ensemble of ten, models enabled us to determine variances and statistically evaluate, bond-length distances and angles in the oxoanions. In total, nine bromate, positions, including two BrO(3)(-) x HBrO(3) dimer species, have been, identified on the basis of the anomalous signal of the Br atoms. For all, bromate ions, the main-chain amide atoms of the protein were identified as, the dominant binding positions, a useful property in any experimental, phase-determination experiment.
Only a few protein-oxoanion crystal complexes have been described to date. Here, the structure of a protein soaked in a bromate solution has been determined to a resolution of 1.25 A and refined to final overall R/R(free) values of 18.04/21.3 (isotropic) and 11.25/14.67 (anisotropic). In contrast to the single-model approach, refinement of an ensemble of ten models enabled us to determine variances and statistically evaluate bond-length distances and angles in the oxoanions. In total, nine bromate positions, including two BrO(3)(-) x HBrO(3) dimer species, have been identified on the basis of the anomalous signal of the Br atoms. For all bromate ions, the main-chain amide atoms of the protein were identified as the dominant binding positions, a useful property in any experimental phase-determination experiment.


==About this Structure==
==About this Structure==
2D6B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL, NA and 202 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D6B OCA].  
2D6B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=202:'>202</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6B OCA].  


==Reference==
==Reference==
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mesters, J.R.]]
[[Category: Mesters, J R.]]
[[Category: Ondracek, J.]]
[[Category: Ondracek, J.]]
[[Category: 202]]
[[Category: 202]]
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[[Category: lysozyme; bromate]]
[[Category: lysozyme; bromate]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:27:56 2007''
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Revision as of 17:55, 21 February 2008

File:2d6b.gif


2d6b, resolution 1.25Å

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Novel Bromate Species trapped within a Protein Crystal

OverviewOverview

Only a few protein-oxoanion crystal complexes have been described to date. Here, the structure of a protein soaked in a bromate solution has been determined to a resolution of 1.25 A and refined to final overall R/R(free) values of 18.04/21.3 (isotropic) and 11.25/14.67 (anisotropic). In contrast to the single-model approach, refinement of an ensemble of ten models enabled us to determine variances and statistically evaluate bond-length distances and angles in the oxoanions. In total, nine bromate positions, including two BrO(3)(-) x HBrO(3) dimer species, have been identified on the basis of the anomalous signal of the Br atoms. For all bromate ions, the main-chain amide atoms of the protein were identified as the dominant binding positions, a useful property in any experimental phase-determination experiment.

About this StructureAbout this Structure

2D6B is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

An ensemble of crystallographic models enables the description of novel bromate-oxoanion species trapped within a protein crystal., Ondracek J, Mesters JR, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):996-1001. Epub 2006, Aug 19. PMID:16929100

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