Gopalasingam, Chai C and Hasnain, S Samar
(2022)
Frontiers in metalloprotein crystallography and cryogenic electron microscopy.
CURRENT OPINION IN STRUCTURAL BIOLOGY, 75.
102420-.
Abstract
Metalloproteins comprise at least a third of all proteins that utilize redox properties of transition metals on their own or as parts of cofactors. The development of third generation storage ring sources and X-ray free-electron lasers with femtosecond pulses in the first decade of the 21st century has transformed metalloprotein crystallography. In the past decade, cryogenic-electron microscopy single-particle analysis, which does not require crystallization of biological samples has been extensively utilized, particularly for membrane-bound metalloprotein systems. Here, we explore recent frontiers in metalloprotein crystallography and cryogenic electron microscopy, organized for convenience under three metalloprotein-centered biological cycles, focusing on contributions from each technique, their synergy and the ability to preserve metals' redox states when subjected to a particular probe.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Metalloproteins, Cryoelectron Microscopy, Crystallization, Crystallography, Crystallography, X-Ray, X-Rays |
| Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 14 Jul 2022 09:12 |
| Last Modified: | 18 Jan 2023 20:56 |
| DOI: | 10.1016/j.sbi.2022.102420 |
| Open Access URL: | https://doi.org/10.1016/j.sbi.2022.102420 |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3158467 |
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