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          Institute: MPI für medizinische Forschung     Collection: Gruppe Moritz Helmstaedter     Display Documents



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ID: 567406.0, MPI für medizinische Forschung / Gruppe Moritz Helmstaedter
X−ray damage to the Mn4Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography
Translation of Title:X−ray damage to the Mn4Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography
Authors:Yano, Junko; Kern, Jana; Irrgang, Klaus−Dieter; Latimer, Matthew J.; Bergmann, Uwe; Glatzel, Pieter; Pushkar, Yulia N.; Biesiadka, Jacek; Loll, Bernhard; Sauer, Kenneth; Messinger, Johannes; Zouni, Athina; Yachandra, Vittal K.
Language:English
Date of Publication (YYYY-MM-DD):2005-08-23
Title of Journal:Proceedings of the National Academy of Sciences of the USA
Journal Abbrev.:PNAS
Volume:102
Issue / Number:34
Start Page:12047
End Page:12052
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:X−ray absorption spectroscopy was used to measure the damage caused by exposure to x−rays to the Mn4Ca active site in single crystals of photosystem II as a function of dose and energy of x−rays, temperature, and time. These studies reveal that the conditions used for structure determination by x−ray crystallography cause serious damage specifically to the metal−site structure. The x−ray absorption spectra show that the structure changes from one that is characteristic of a high−valent Mn4(III2,IV2) oxo−bridged Mn4Ca cluster to that of Mn(II) in aqueous solution. This damage to the metal site occurs at a dose that is more than one order of magnitude lower than the dose that results in loss of diffractivity and is commonly considered safe for protein crystallography. These results establish quantitative x−ray dose parameters that are applicable to redox−active metalloproteins. This case study shows that a careful evaluation of the structural intactness of the active site(s) by spectroscopic techniques can validate structures derived from crystallography and that it can be a valuable complementary method before structureÃÆ'¢â‚¬â€œfunction correlations of metalloproteins can be made on the basis of high−resolution x−ray crystal structures
Free Keywords:manganese, oxygen evolution, water oxidation, X−ray spectroscopy
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomedizinische Optik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomedizinische Optik/Gruppe Moritz Helmstaedter
Identifiers:LOCALID:6458
URI:http%3A%2F%2Fwww.pnas.org%2Fcgi%2Freprint%2F102%2F...
URI:http%3A%2F%2Fwww.pnas.org%2Fcgi%2Fcontent%2Ffull%2...
URI:http%3A%2F%2Fwww.pnas.org%2Fcgi%2Fcontent%2Fabstra...
DOI:10.1073%2Fpnas.0505207102
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