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''' | ==Spectroscopically-validated structure of cytochrome c prime from Alcaligenes xylosoxidans, reduced by X-ray irradiation at 100K== | ||
<StructureSection load='4cdv' size='340' side='right' caption='[[4cdv]], [[Resolution|resolution]] 1.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4cdv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CDV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CDV FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cda|4cda]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cdv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cdv RCSB], [http://www.ebi.ac.uk/pdbsum/4cdv PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
It is crucial to assign the correct redox and ligand states to crystal structures of proteins with an active redox centre to gain valid functional information and prevent the misinterpretation of structures. Single-crystal spectroscopies, particularly when applied in situ at macromolecular crystallography beamlines, allow spectroscopic investigations of redox and ligand states and the identification of reaction intermediates in protein crystals during the collection of structural data. Single-crystal resonance Raman spectroscopy was carried out in combination with macromolecular crystallography on Swiss Light Source beamline X10SA using cytochrome c' from Alcaligenes xylosoxidans. This allowed the fingerprinting and validation of different redox and ligand states, identification of vibrational modes and identification of intermediates together with monitoring of radiation-induced changes. This combined approach provides a powerful tool to obtain complementary data and correctly assign the true oxidation and ligand state(s) in redox-protein crystals. | |||
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy.,Kekilli D, Dworkowski FS, Pompidor G, Fuchs MR, Andrew CR, Antonyuk S, Strange RW, Eady RR, Hasnain SS, Hough MA Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1289-96. doi:, 10.1107/S1399004714004039. Epub 2014 Apr 29. PMID:24816098<ref>PMID:24816098</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Antonyuk, S.]] | |||
[[Category: Dworkowski, F.]] | |||
[[Category: Hough, M A.]] | |||
[[Category: Kekilli, D.]] | |||
[[Category: Electron transport]] | |||
[[Category: Ferric]] | |||
[[Category: Gas sensor]] | |||
[[Category: Haem]] | |||
[[Category: Heme]] | |||
[[Category: Ligand discrimination]] | |||
[[Category: Radiolysis]] | |||
[[Category: Resonance raman]] | |||
[[Category: Validation]] | |||
Revision as of 12:08, 21 May 2014
Spectroscopically-validated structure of cytochrome c prime from Alcaligenes xylosoxidans, reduced by X-ray irradiation at 100KSpectroscopically-validated structure of cytochrome c prime from Alcaligenes xylosoxidans, reduced by X-ray irradiation at 100K
Structural highlights
Publication Abstract from PubMedIt is crucial to assign the correct redox and ligand states to crystal structures of proteins with an active redox centre to gain valid functional information and prevent the misinterpretation of structures. Single-crystal spectroscopies, particularly when applied in situ at macromolecular crystallography beamlines, allow spectroscopic investigations of redox and ligand states and the identification of reaction intermediates in protein crystals during the collection of structural data. Single-crystal resonance Raman spectroscopy was carried out in combination with macromolecular crystallography on Swiss Light Source beamline X10SA using cytochrome c' from Alcaligenes xylosoxidans. This allowed the fingerprinting and validation of different redox and ligand states, identification of vibrational modes and identification of intermediates together with monitoring of radiation-induced changes. This combined approach provides a powerful tool to obtain complementary data and correctly assign the true oxidation and ligand state(s) in redox-protein crystals. Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy.,Kekilli D, Dworkowski FS, Pompidor G, Fuchs MR, Andrew CR, Antonyuk S, Strange RW, Eady RR, Hasnain SS, Hough MA Acta Crystallogr D Biol Crystallogr. 2014 May;70(Pt 5):1289-96. doi:, 10.1107/S1399004714004039. Epub 2014 Apr 29. PMID:24816098[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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