R
Robin L. Owen
Researcher at Paul Scherrer Institute
Publications - 96
Citations - 3791
Robin L. Owen is an academic researcher from Paul Scherrer Institute. The author has contributed to research in topics: Beamline & Medicine. The author has an hindex of 31, co-authored 85 publications receiving 3278 citations. Previous affiliations of Robin L. Owen include Rutherford Appleton Laboratory & University of Oxford.
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Journal ArticleDOI
A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
Xiangxi Wang,Wei Peng,Jingshan Ren,Zhongyu Hu,Jiwei Xu,Zhiyong Lou,Xumei Li,Weidong Yin,Xinliang Shen,Claudine Porta,Thomas S. Walter,Gwyndaf Evans,Danny Axford,Robin L. Owen,David J. Rowlands,Junzhi Wang,David I. Stuart,Elizabeth E. Fry,Zihe Rao,Zihe Rao +19 more
TL;DR: These structures provide a model for enterovirus uncoating in which the VP1 GH loop acts as an adaptor-sensor for cellular receptor attachment, converting heterologous inputs to a generic uncoated mechanism, highlighting new opportunities for therapeutic intervention.
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Experimental determination of the radiation dose limit for cryocooled protein crystals
TL;DR: The calculated dose limit of 2 x 10(7) Gy for the diffracting power of cryocooled protein crystals to drop by half has been experimentally evaluated at a third-generation synchrotron source.
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Clustering procedures for the optimal selection of data sets from multiple crystals in macromolecular crystallography
James Foadi,Pierre Aller,Yilmaz Alguel,Alexander D. Cameron,Danny Axford,Robin L. Owen,Wes Armour,David G. Waterman,So Iwata,Gwyndaf Evans +9 more
TL;DR: A systematic approach to the scaling and merging of data from multiple crystals in macromolecular crystallography is introduced and explained.
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Cryocooling and radiation damage in macromolecular crystallography
Elspeth F. Garman,Robin L. Owen +1 more
TL;DR: The current limited understanding of radiation damage in cryocooled crystals, investigations aimed at minimizing its effects and some developments which actually utilize it both for phasing and to extend structural knowledge are summarized.
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Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications
Christian Tiede,Anna A Tang,Sarah E. Deacon,Upasana Mandal,Joanne E. Nettleship,Joanne E. Nettleship,Robin L. Owen,Suja E. George,D Harrison,Raymond J. Owens,Raymond J. Owens,Darren C. Tomlinson,Michael J. McPherson +12 more
TL;DR: Adhirons are highly stable and well expressed allowing highly specific binding reagents to be selected for use in molecular recognition applications and identified binders against >100 target molecules to date.