M
Matthew P. Blakeley
Researcher at European Bioinformatics Institute
Publications - 94
Citations - 2355
Matthew P. Blakeley is an academic researcher from European Bioinformatics Institute. The author has contributed to research in topics: Neutron & Neutron diffraction. The author has an hindex of 27, co-authored 88 publications receiving 2071 citations.
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Journal ArticleDOI
Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study.
Andrey Kovalevsky,Leif Hanson,S. Zoë Fisher,Marat Mustyakimov,Sax A. Mason,V. Trevor Forsyth,Matthew P. Blakeley,David A. Keen,Trixie Wagner,H. L. Carrell,Amy K. Katz,Jenny P. Glusker,Paul Langan,Paul Langan +13 more
TL;DR: The structure of the metalloenzyme D-xylose isomerase is determined by neutron diffraction in order to locate H atoms (or their isotope D) and the results lead to new suggestions as to how changes might take place over the course of the reaction.
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Neutron crystallography: opportunities, challenges, and limitations
TL;DR: In this review of recently determined neutron structures, a theme emerges of a field currently expanding beyond its traditional boundaries, to address larger and more complex problems, with smaller samples and shorter data collection times, and employing more sophisticated structure determination and refinement methods.
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Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase
Cecilia M. Casadei,Andrea Gumiero,Clive Metcalfe,Emma J. Murphy,Jaswir Basran,Maria Grazia Concilio,Susana C. M. Teixeira,Tobias E. Schrader,Alistair J. Fielding,Andreas Ostermann,Matthew P. Blakeley,Emma Lloyd Raven,Peter C. E. Moody +12 more
TL;DR: In this paper, the ferric derivative of cytochrome c peroxidase and its ferryl intermediate are shown to be an Fe(IV)-O species and are not protonated.
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Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential
TL;DR: Neutron crystallography and sub-atomic X-ray crystallography complement each other in defining hydrogen positions in macromolecules and much effort is still required to become a mainstream activity.
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Neutron macromolecular crystallography
TL;DR: Neutron macromolecular crystallography as discussed by the authors has led to an expanding field addressing larger and more complex problems, such as direct determination of the position of the proton and deuteron positions and their bound solvent.