Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Briony A. Yorke"'
Autor:
Jake A. Hill, Yvonne Nyathi, Sam Horrell, David von Stetten, Danny Axford, Robin L. Owen, Godfrey S. Beddard, Arwen R. Pearson, Helen M. Ginn, Briony A. Yorke
Publikováno v:
Communications Chemistry, Vol 7, Iss 1, Pp 1-8 (2024)
Abstract Human gamma-D crystallin (HGD) is a major constituent of the eye lens. Aggregation of HGD contributes to cataract formation, the leading cause of blindness worldwide. It is unique in its longevity, maintaining its folded and soluble state fo
Externí odkaz:
https://doaj.org/article/a7a4539ed52244a9845ffd7debe82e95
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
'Acta Crystallographica D ', vol: 78, pages: 14-29 (2022)
'Acta Crystallographica D ', vol: 78, pages: 14-29 (2022)
The key factors that should be considered during the planning and execution of a time-resolved crystallographic experiment are discussed, with a focus on time-resolved serial synchrotron crystallography.
With recent developments in X-ray sources
With recent developments in X-ray sources
Autor:
Tushar Raskar, Stephan Niebling, Juliette M. Devos, Briony A. Yorke, Michael Härtlein, Nils Huse, V. Trevor Forsyth, Tilo Seydel, Arwen R. Pearson
Incoherent neutron spectroscopy, in combination with dynamic light scattering, was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics of Escherichia coli aspartate α-decarboxylase (A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4746d91287d547030bb9fef59c3ef5b0
https://eprints.keele.ac.uk/11390/1/d2cp02063g.pdf
https://eprints.keele.ac.uk/11390/1/d2cp02063g.pdf
Autor:
Yonca Yuzugullu Karakus, Arwen R. Pearson, Briony A. Yorke, Chi H. Trinh, S. Balci, Gunce Goc, Michael J. McPherson
Publikováno v:
'Acta Crystallographica D ', vol: 74, pages: 979-985 (2018)
Acta Crystallographica. Section D, Structural Biology
Acta Crystallographica. Section D, Structural Biology
The structure of Scytalidium thermophilum catalase in complex with its well known inhibitor 3-amino-1,2,4-triazole revealed that the inhibitor occupies a surface pocket at the end of the lateral channel. This pocket corresponds to the site of NADPH b
Autor:
Tilo Seydel, Briony A. Yorke, Stephan Niebling, Arwen R. Pearson, Nils Huse, Raskar T, Juliette M. Devos, V.T. Forsyth, Härtlein M
Incoherent neutron spectroscopy, in combination with dynamic light scattering was used to investigate the effect of ligand binding on the center-of-mass self-diffusion and internal diffusive dynamics ofE.coliaspartateα-decarboxylase (ADC). The X-ray
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::95bb18e162f56c5ba02a26d1df71c530
https://doi.org/10.1101/2020.08.11.244939
https://doi.org/10.1101/2020.08.11.244939
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1869:140662
Scytalidium catalase is a homotetramer including heme d in each subunit. Its primary function is the dismutation of H2O2 to water and oxygen, but it is also able to oxidase various small organic compounds including catechol and phenol. The crystal st
Autor:
Briony A. Yorke, Arwen R. Pearson, John J. Zaitsev-Doyle, Marta Sans, Henrike M. Müller-Werkmeister, Yannik Pfeifer, Hao Yan, Nils Huse, Anke Puchert, Julia Rehbein, Charlotte Uetrecht
We report a new synthetic route to a series of a-carboxynitrobenzyl photocaged L-aspartates for application in time-resolved structural biology. The resulting compounds were characterised in terms of UV/Vis absorption properties, aqueous solubility a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4cd097cce45ce06c28da838f897d1d1
https://eprints.whiterose.ac.uk/146467/7/c9ra00968j.pdf
https://eprints.whiterose.ac.uk/146467/7/c9ra00968j.pdf
Autor:
Arwen R. Pearson, Nils Huse, Briony A. Yorke, Charlotte Uetrecht, Henning Tidow, Anke Puchert, Stephanie Kesgin‐Schaefer, Knut Koelbel, Johannes Heidemann
Publikováno v:
The FEBS Journal
Photoactivatable fluorescent proteins (PA-FPs) are a powerful non-invasive tool in high-resolution live-cell imaging. They can be converted from an inactive to an active form by light, enabling the spatial and temporal trafficking of proteins and cel
Autor:
Jochen Meyer, Eike C. Schulz, Thomas R. Schneider, Stefan Fiedler, Maxim Polikarpov, Diana C. F. Monteiro, Nils Huse, Sam Horrell, Marina Nikolova, Arwen R. Pearson, Ivars Karpics, Godfrey S. Beddard, Briony A. Yorke, Pedram Mehrabi, Martin Trebbin, R. J. Dwayne Miller, Uwe Ristau, Friedjof Tellkamp, Gleb Bourenkov, David von Stetten, Thomas Gehrmann, Michael Agthe
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 75:e26-e26
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 68:505-510
During X-ray irradiation protein crystals radiate energy in the form of small amounts of visible light. This is known as X-ray-excited optical luminescence (XEOL). The XEOL of several proteins and their constituent amino acids has been characterized