Work

Crystallography with X-ray and optical spectroscopies for metalloproteins structural studies

Year: 2008

Type: article

Abstract: Microsymposiafold increase in dose.Comparing structural results from EXAFS to those from crystallography on this and similar proteins, show that x-ray induced photoreduction has impacted the crystallographic data and subsequent structure solutions.These results indicate the importance of using LHe-based cooling for metalloprotein crystallography in order to limit changes at the metalloprotein active sites.The study also illustrates the need for direct measurement of redox states of the metals, through XAS, simultaneously with the crystallographic measurements.The work was performed at SSRL with support from the NIH NCRR BTP program and the US DOE BER.SSRL operations are

Source: Acta Crystallographica Section A Foundations of Crystallography

DOI: 10.1107/s0108767308096487

Authors: S. Hasnain, R. Strange, M. Hough, R. Eady, S. Antonyuk, M. Ellis

Institutions: University of Liverpool, National Institute of Advanced Industrial Science and Technology, Daresbury Laboratory

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: bronze

Funders: U.S. Department of Energy, National Institutes of Health, National Center for Research Resources

OpenAlex ID: W2318823317