Zobrazeno 1 - 10
of 127
pro vyhledávání: '"Michael A. Hough"'
Autor:
Halina Mikolajek, Juan Sanchez-Weatherby, James Sandy, Richard J. Gildea, Ivan Campeotto, Harish Cheruvara, John D. Clarke, Toshana Foster, Sotaro Fujii, Ian T. Paulsen, Bhumika S. Shah, Michael A. Hough
Publikováno v:
IUCrJ, Vol 10, Iss 4, Pp 420-429 (2023)
The utility of X-ray crystal structures determined under ambient-temperature conditions is becoming increasingly recognized. Such experiments can allow protein dynamics to be characterized and are particularly well suited to challenging protein targe
Externí odkaz:
https://doaj.org/article/8fb617325645451bb51a64b3a87fa551
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:
Frontiers in Molecular Biosciences, Vol 10 (2023)
The interaction between macromolecular proteins and small molecule ligands is an essential component of cellular function. Such ligands may include enzyme substrates, molecules involved in cellular signalling or pharmaceutical drugs. Together with bi
Externí odkaz:
https://doaj.org/article/0ef51fc8b5c94b60b1f1fce88618c681
Autor:
Boyd A. McKew, Richard Johnson, Lindsay Clothier, Karl Skeels, Matthew S. Ross, Metodi Metodiev, Max Frenzel, Lisa M. Gieg, Jonathan W. Martin, Michael A. Hough, Corinne Whitby
Publikováno v:
MicrobiologyOpen, Vol 10, Iss 4, Pp n/a-n/a (2021)
Abstract Naphthenic acids (NAs) are carboxylic acids with the formula (CnH2n+ZO2) and are among the most toxic, persistent constituents of oil sands process‐affected waters (OSPW), produced during oil sands extraction. Currently, the proteins and m
Externí odkaz:
https://doaj.org/article/d6c7cb15be004fdab001ceb53f918a98
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:
Kakali Sen, Sam Horrell, Demet Kekilli, Chin W. Yong, Thomas W. Keal, Hakan Atakisi, David W. Moreau, Robert E. Thorne, Michael A. Hough, Richard W. Strange
Publikováno v:
IUCrJ, Vol 4, Iss 4, Pp 495-505 (2017)
Microbial nitrite reductases are denitrifying enzymes that are a major component of the global nitrogen cycle. Multiple structures measured from one crystal (MSOX data) of copper nitrite reductase at 240 K, together with molecular-dynamics simulation
Externí odkaz:
https://doaj.org/article/c83a0998fa7a460383aad55bceb65f6d
Autor:
Demet Kekilli, Tadeo Moreno-Chicano, Amanda K. Chaplin, Sam Horrell, Florian S. N. Dworkowski, Jonathan A. R. Worrall, Richard W. Strange, Michael A. Hough
Publikováno v:
IUCrJ, Vol 4, Iss 3, Pp 263-270 (2017)
Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into r
Externí odkaz:
https://doaj.org/article/8b2bf4548c0b4d05886fcd59e4cd3373
Autor:
Sam Horrell, Svetlana V. Antonyuk, Robert R. Eady, S. Samar Hasnain, Michael A. Hough, Richard W. Strange
Publikováno v:
IUCrJ, Vol 3, Iss 4, Pp 271-281 (2016)
Relating individual protein crystal structures to an enzyme mechanism remains a major and challenging goal for structural biology. Serial crystallography using multiple crystals has recently been reported in both synchrotron-radiation and X-ray free-
Externí odkaz:
https://doaj.org/article/434ddd5033b24b76b98c35d07d3ccdb2