X-ray damage to the Mn <sub>4</sub> Ca complex in single crystals of photosystem II: A case study for metalloprotein crystallography

Junko Yano(Stanford Synchrotron Radiation Lightsource), Jan Kern(Stanford Synchrotron Radiation Lightsource), Klaus‐Dieter Irrgang(Stanford Synchrotron Radiation Lightsource), Matthew J. Latimer(Stanford Synchrotron Radiation Lightsource), Uwe Bergmann(Stanford Synchrotron Radiation Lightsource), Pieter Glatzel(Stanford Synchrotron Radiation Lightsource), Yulia Pushkar(Stanford Synchrotron Radiation Lightsource), Jacek Biesiadka(Stanford Synchrotron Radiation Lightsource), Bernhard Loll(Stanford Synchrotron Radiation Lightsource), Kenneth Sauer(Stanford Synchrotron Radiation Lightsource), Johannes Messinger(Stanford Synchrotron Radiation Lightsource), Athina Zouni(Stanford Synchrotron Radiation Lightsource), Vittal K. Yachandra(Stanford Synchrotron Radiation Lightsource)
Proceedings of the National Academy of Sciences
August 15, 2005
Cited by 584Open Access
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Abstract

X-ray absorption spectroscopy was used to measure the damage caused by exposure to x-rays to the Mn(4)Ca 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 Mn(4)(III(2),IV(2)) oxo-bridged Mn(4)Ca 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 structure-function correlations of metalloproteins can be made on the basis of high-resolution x-ray crystal structures.


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