Research Repository

Monitoring and validating active site redox states in protein crystals

Antonyuk, SV and Hough, MA (2011) 'Monitoring and validating active site redox states in protein crystals.' Biochimica et Biophysica Acta - Proteins and Proteomics, 1814 (6). 778 - 784. ISSN 1570-9639

Full text not available from this repository.

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
Subjects: Q Science > Q Science (General)
Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Mike Hough
Date Deposited: 04 Aug 2011 15:27
Last Modified: 10 Sep 2019 11:15
URI: http://repository.essex.ac.uk/id/eprint/378

Actions (login required)

View Item View Item