Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Robin L. Owen"'
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
Autor:
Tadeo Moreno-Chicano, Leiah M. Carey, Danny Axford, John H. Beale, R. Bruce Doak, Helen M. E. Duyvesteyn, Ali Ebrahim, Robert W. Henning, Diana C. F. Monteiro, Dean A. Myles, Shigeki Owada, Darren A. Sherrell, Megan L. Straw, Vukica Šrajer, Hiroshi Sugimoto, Kensuke Tono, Takehiko Tosha, Ivo Tews, Martin Trebbin, Richard W. Strange, Kevin L. Weiss, Jonathan A. R. Worrall, Flora Meilleur, Robin L. Owen, Reza A. Ghiladi, Michael A. Hough
Publikováno v:
IUCrJ, Vol 9, Iss 5, Pp 610-624 (2022)
Room-temperature macromolecular crystallography allows protein structures to be determined under close-to-physiological conditions, permits dynamic freedom in protein motions and enables time-resolved studies. In the case of metalloenzymes that are h
Externí odkaz:
https://doaj.org/article/288bb78b21864584a71fa98e261fa74e
Publikováno v:
IUCrJ, Vol 8, Iss 6, Pp 896-904 (2021)
X-ray-induced radiation damage is a limiting factor for the macromolecular crystallographer and data must often be merged from many crystals to yield complete data sets for the structure solution of challenging samples. Increasing the X-ray energy be
Externí odkaz:
https://doaj.org/article/a9b61fdbda464a97ac4b18878e62cd8c
Autor:
Agata Butryn, Philipp S. Simon, Pierre Aller, Philip Hinchliffe, Ramzi N. Massad, Gabriel Leen, Catherine L. Tooke, Isabel Bogacz, In-Sik Kim, Asmit Bhowmick, Aaron S. Brewster, Nicholas E. Devenish, Jürgen Brem, Jos J. A. G. Kamps, Pauline A. Lang, Patrick Rabe, Danny Axford, John H. Beale, Bradley Davy, Ali Ebrahim, Julien Orlans, Selina L. S. Storm, Tiankun Zhou, Shigeki Owada, Rie Tanaka, Kensuke Tono, Gwyndaf Evans, Robin L. Owen, Frances A. Houle, Nicholas K. Sauter, Christopher J. Schofield, James Spencer, Vittal K. Yachandra, Junko Yano, Jan F. Kern, Allen M. Orville
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-7 (2021)
Currently many of the time resolved serial femtosecond (SFX) crystallography experiments are done with light driven protein systems, whereas the reaction initiation for non-light triggered enzymes remains a major bottle neck. Here, the authors presen
Externí odkaz:
https://doaj.org/article/55ce2079723b464484f4eed86828b06d
Autor:
Patrick Rabe, John H. Beale, Agata Butryn, Pierre Aller, Anna Dirr, Pauline A. Lang, Danny N. Axford, Stephen B. Carr, Thomas M. Leissing, Michael A. McDonough, Bradley Davy, Ali Ebrahim, Julien Orlans, Selina L. S. Storm, Allen M. Orville, Christopher J. Schofield, Robin L. Owen
Publikováno v:
IUCrJ, Vol 7, Iss 5, Pp 901-912 (2020)
Cryogenic X-ray diffraction is a powerful tool for crystallographic studies on enzymes including oxygenases and oxidases. Amongst the benefits that cryo-conditions (usually employing a nitrogen cryo-stream at 100 K) enable, is data collection of diox
Externí odkaz:
https://doaj.org/article/541ddf2ff1b14f87878d1b366c92c115
Autor:
Tadeo Moreno-Chicano, Ali Ebrahim, Danny Axford, Martin V. Appleby, John H. Beale, Amanda K. Chaplin, Helen M. E. Duyvesteyn, Reza A. Ghiladi, Shigeki Owada, Darren A. Sherrell, Richard W. Strange, Hiroshi Sugimoto, Kensuke Tono, Jonathan A. R. Worrall, Robin L. Owen, Michael A. Hough
Publikováno v:
IUCrJ, Vol 6, Iss 6, Pp 1074-1085 (2019)
High-throughput X-ray crystal structures of protein–ligand complexes are critical to pharmaceutical drug development. However, cryocooling of crystals and X-ray radiation damage may distort the observed ligand binding. Serial femtosecond crystallog
Externí odkaz:
https://doaj.org/article/ad7f2d9a92a74ab3b6301d2289377fb5
Autor:
Ali Ebrahim, Tadeo Moreno-Chicano, Martin V. Appleby, Amanda K. Chaplin, John H. Beale, Darren A. Sherrell, Helen M. E. Duyvesteyn, Shigeki Owada, Kensuke Tono, Hiroshi Sugimoto, Richard W. Strange, Jonathan A. R. Worrall, Danny Axford, Robin L. Owen, Michael A. Hough
Publikováno v:
IUCrJ, Vol 6, Iss 4, Pp 543-551 (2019)
An approach is demonstrated to obtain, in a sample- and time-efficient manner, multiple dose-resolved crystal structures from room-temperature protein microcrystals using identical fixed-target supports at both synchrotrons and X-ray free-electron la
Externí odkaz:
https://doaj.org/article/d85919f46169431f8075520a1390d09b
Autor:
Sam Horrell, Demet Kekilli, Kakali Sen, Robin L. Owen, Florian S. N. Dworkowski, Svetlana V. Antonyuk, Thomas W. Keal, Chin W. Yong, Robert R. Eady, S. Samar Hasnain, Richard W. Strange, Michael A. Hough
Publikováno v:
IUCrJ, Vol 5, Iss 3, Pp 283-292 (2018)
High-resolution crystal structures of enzymes in relevant redox states have transformed our understanding of enzyme catalysis. Recent developments have demonstrated that X-rays can be used, via the generation of solvated electrons, to drive reactions
Externí odkaz:
https://doaj.org/article/85e6dbab74a14cc1ad0ccf5a3383c86d
Autor:
Marina Lučić, Michael T. Wilson, Takehiko Tosha, Hiroshi Sugimoto, Anastasya Shilova, Danny Axford, Robin L. Owen, Michael A. Hough, Jonathan A. R. Worrall
Publikováno v:
ACS Catalysis. 12:13349-13359
Controlling the reactivity of high-valent Fe(IV)-O catalytic intermediates, Compounds I and II, generated in heme enzymes upon reaction with dioxygen or hydrogen peroxide, is important for function. It has been hypothesized that the presence (wet) or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1143286b5de678d14508672047bcbf2
https://doi.org/10.1021/acscatal.2c03754
https://doi.org/10.1021/acscatal.2c03754
Autor:
Rachel Bolton, Moritz M. Machelett, Jack Stubbs, Danny Axford, Nicolas Caramello, Lucrezia Catapano, Martin Malý, Matthew J. Rodrigues, Charlotte Cordery, Graham J. Tizzard, Fraser MacMillan, Sylvain Engilberge, David von Stetten, Takehiko Tosha, Hiroshi Sugimoto, Jonathan A.R. Worrall, Jeremy S. Webb, Mike Zubkov, Simon Coles, Eric Mathieu, Roberto A. Steiner, Garib Murshudov, Tobias E. Schrader, Allen M. Orville, Antoine Royant, Gwyndaf Evans, Michael A. Hough, Robin L. Owen, Ivo Tews
The marine cyanobacteriumProchlorococcusis a main contributor to global photosynthesis, whilst being limited by iron availability. Cyanobacterial genomes typically encode two different types of FutA iron binding proteins: periplasmic FutA2 ABC transp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a1b7531313669316f8de3cadce45f50
https://doi.org/10.1101/2023.05.23.541926
https://doi.org/10.1101/2023.05.23.541926
