Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis

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Abstract

An estimated half of all proteins contain a metal, with these being essential for a tremendous variety of biological functions. X-ray crystallography is the major method for obtaining structures at high resolution of these metalloproteins, but there are considerable challenges to obtain intact structures due to the effects of radiation damage. Serial crystallography offers the prospect of determining low-dose synchrotron or effectively damage free XFEL structures at room temperature and enables time-resolved or dose-resolved approaches. Complementary spectroscopic data can validate redox and or ligand states within metalloprotein crystals. In this opinion, we discuss developments in the application of serial crystallographic approaches to metalloproteins and comment on future directions.

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Metalloproteins and metal sensing.

Kevin Waldron, Julian C Rutherford, Dianne Ford … (2009)

Almost half of all enzymes must associate with a particular metal to function. An ambition is to understand why each metal-protein partnership arose and how it is maintained. Metal availability provides part of the explanation, and has changed over geological time and varies between habitats but is held within vital limits in cells. Such homeostasis needs metal sensors, and there is an ongoing search to discover the metal-sensing mechanisms. For metalloproteins to acquire the right metals, metal sensors must correctly distinguish between the inorganic elements.

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Potential for biomolecular imaging with femtosecond X-ray pulses.

Richard Neutze, Remco Wouts, David van der Spoel … (2000)

Sample damage by X-rays and other radiation limits the resolution of structural studies on non-repetitive and non-reproducible structures such as individual biomolecules or cells. Cooling can slow sample deterioration, but cannot eliminate damage-induced sample movement during the time needed for conventional measurements. Analyses of the dynamics of damage formation suggest that the conventional damage barrier (about 200 X-ray photons per A2 with X-rays of 12 keV energy or 1 A wavelength) may be extended at very high dose rates and very short exposure times. Here we have used computer simulations to investigate the structural information that can be recovered from the scattering of intense femtosecond X-ray pulses by single protein molecules and small assemblies. Estimations of radiation damage as a function of photon energy, pulse length, integrated pulse intensity and sample size show that experiments using very high X-ray dose rates and ultrashort exposures may provide useful structural information before radiation damage destroys the sample. We predict that such ultrashort, high-intensity X-ray pulses from free-electron lasers that are currently under development, in combination with container-free sample handling methods based on spraying techniques, will provide a new approach to structural determinations with X-rays.

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Is Open Access

Serial femtosecond crystallography: the first five years

Ilme Schlichting (2015)

The advent of hard X-ray free-electron lasers has opened a new chapter in macromolecular crystallography. Recent results, developments and prospects of serial femtosecond crystallography are described.

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Author and article information

Contributors

Michael A. Hough

Robin L. Owen

Journal

Journal ID (nlm-ta): Curr Opin Struct Biol

Journal ID (iso-abbrev): Curr Opin Struct Biol

Title: Current Opinion in Structural Biology

Publisher: Elsevier Science

ISSN (Print): 0959-440X

ISSN (Electronic): 1879-033X

Publication date PMC-release: 1 December 2021

Publication date (Print): December 2021

Volume: 71

Pages: 232-238

Affiliations

[1 ]School of Life Sciences, University of Essex, Wivenhoe Park, Colchester, CO4 3SQ, UK

[2 ]Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, UK

Author notes

[∗ ]Corresponding author: Hough, Michael A mahough@ 123456essex.ac.uk

[∗∗ ]Corresponding author: Owen, Robin L robin.owen@ 123456diamond.ac.uk

Article

Publisher Item ID: S0959-440X(21)00109-3

DOI: 10.1016/j.sbi.2021.07.007

PMC ID: 8667872

PubMed ID: 34455163

SO-VID: fc3339c7-7a6f-4c9c-a741-7538bf4f0bd0

License:

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

Serial synchrotron and XFEL crystallography for studies of metalloprotein catalysis

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Most cited references 47

Metalloproteins and metal sensing.

Potential for biomolecular imaging with femtosecond X-ray pulses.

Serial femtosecond crystallography: the first five years

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