Antonyuk, Svetlana V and Hough, Michael A (2011) Monitoring and validating active site redox states in protein crystals. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1814 (6). pp. 778-784. DOI https://doi.org/10.1016/j.bbapap.2010.12.017
Antonyuk, Svetlana V and Hough, Michael A (2011) Monitoring and validating active site redox states in protein crystals. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1814 (6). pp. 778-784. DOI https://doi.org/10.1016/j.bbapap.2010.12.017
Antonyuk, Svetlana V and Hough, Michael A (2011) Monitoring and validating active site redox states in protein crystals. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1814 (6). pp. 778-784. DOI https://doi.org/10.1016/j.bbapap.2010.12.017
Abstract
High resolution protein crystallography using synchrotron radiation is one of the most powerful tools in modern biology. Improvements in resolution have arisen from the use of X-ray beamlines with higher brightness and flux and the development of advanced detectors. However, it is increasingly recognised that the benefits brought by these advances have an associated cost, namely deleterious effects of X-ray radiation on the sample (radiation damage). In particular, X-ray induced reduction and damage to redox centres has been shown to occur much more rapidly than other radiation damage effects, such as loss of resolution or damage to disulphide bridges. Selection of an appropriate combination of in-situ single crystal spectroscopies during crystallographic experiments, such as UV-visible absorption and X-ray absorption spectroscopy (XAFS), allows for effective monitoring of redox states in protein crystals in parallel with structure determination. Such approaches are also essential in cases where catalytic intermediate species are generated by exposure to the X-ray beam. In this article, we provide a number of examples in which multiple single crystal spectroscopies have been key to understanding the redox status of Fe and Cu centres in crystal structures. This article is part of a Special Issue entitled: Protein Structure and Function in the Crystalline State. © 2010 Elsevier B.V. All rights reserved.
Item Type: | Article |
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Uncontrolled Keywords: | Redox protein; Metalloprotein; Structure validation; Combined method; XAS; Spectroscopy |
Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 04 Aug 2011 15:27 |
Last Modified: | 30 Oct 2024 17:06 |
URI: | http://repository.essex.ac.uk/id/eprint/378 |