Zobrazeno 1 - 10
of 117
pro vyhledávání: '"Serial synchrotron crystallography"'
Autor:
Guillaume Gotthard, Sandra Mous, Tobias Weinert, Raiza Nara Antonelli Maia, Daniel James, Florian Dworkowski, Dardan Gashi, Antonia Furrer, Dmitry Ozerov, Ezequiel Panepucci, Meitian Wang, Gebhard F. X. Schertler, Joachim Heberle, Joerg Standfuss, Przemyslaw Nogly
Publikováno v:
IUCrJ, Vol 11, Iss 5, Pp 792-808 (2024)
Light–oxygen–voltage (LOV) domains are small photosensory flavoprotein modules that allow the conversion of external stimuli (sunlight) into intracellular signals responsible for various cell behaviors (e.g. phototropism and chloroplast relocatio
Externí odkaz:
https://doaj.org/article/0487f96a71db49698c8ff3e32bc949bf
Autor:
Yongsam Kim, Ki Hyun Nam
Publikováno v:
Data in Brief, Vol 55, Iss , Pp 110604- (2024)
Pink-beam serial synchrotron crystallography (SSX) is beneficial in terms of X-ray flux and overcoming partial reflection compared with SSX using a monochromatic beam. The fixed-target (FT) scanning method can minimize the physical damage on the crys
Externí odkaz:
https://doaj.org/article/29f100465d9c47bdb5c027ac5dd5a404
Autor:
Marius Schmidt
Publikováno v:
IUCrJ, Vol 11, Iss 5, Pp 645-646 (2024)
The photo-reaction of the LOV1 domain of the Chlamydomonas reinhardtii phototropin is investigated by room-temperature time-resolved serial crystallography. A covalent adduct forms between the C4a atom of the central flavin-mononucleotide chromophore
Externí odkaz:
https://doaj.org/article/5479d9275b5743c2b471a8869598b936
Autor:
Ki Hyun Nam
Publikováno v:
Data in Brief, Vol 52, Iss , Pp 110055- (2024)
The endo-1,4-β-xylanase GH11 from the hemicellulose-degrading bacterium Thermoanaerobacterium saccharolyticum (TsaGH11) has been characterized as a thermophilic enzyme. TsaGH11 exhibits its maximum activity at pH 5.0 and 70 °C, along with superior
Externí odkaz:
https://doaj.org/article/79f4ab44c0ca41e79097fda17eace509
Autor:
Yongsam Kim, Ki Hyun Nam
Publikováno v:
Data in Brief, Vol 52, Iss , Pp 109811- (2024)
Serial synchrotron crystallography (SSX) helps to determine the room-temperature structure of macromolecules with minimal radiation damage. Pink-beam X-ray provides more photon flux than a monochromatic beam, which can increase the diffraction intens
Externí odkaz:
https://doaj.org/article/5044fc28acaa4df39f1c75e486279ce8
Autor:
Ki Hyun Nam
Publikováno v:
Current Research in Structural Biology, Vol 7, Iss , Pp 100131- (2024)
Serial crystallography (SX) is an emerging technique that can be used to determine the noncryogenic crystal structure of macromolecules while minimizing radiation damage. Applying SX using pump-probe or mix-and-inject techniques enables the observati
Externí odkaz:
https://doaj.org/article/175f4cd992c44e9e99f848d1f370e156
Autor:
Feng-Zhu Zhao, Zhi-Jun Wang, Qing-Jie Xiao, Li Yu, Bo Sun, Qian Hou, Liang-Liang Chen, Huan Liang, Hai Wu, Wei-Hong Guo, Jian-Hua He, Qi-Sheng Wang, Da-Chuan Yin
Publikováno v:
Journal of Synchrotron Radiation, Vol 30, Iss 2, Pp 347-358 (2023)
There is an increasing demand for simple and efficient sample delivery technology to match the rapid development of serial crystallography and its wide application in analyzing the structural dynamics of biological macromolecules. Here, a microfluidi
Externí odkaz:
https://doaj.org/article/76edfcafa19445ae9b82988471a0a160
Autor:
Darren A. Sherrell, Alex Lavens, Mateusz Wilamowski, Youngchang Kim, Ryan Chard, Krzysztof Lazarski, Gerold Rosenbaum, Rafael Vescovi, Jessica L. Johnson, Chase Akins, Changsoo Chang, Karolina Michalska, Gyorgy Babnigg, Ian Foster, Andrzej Joachimiak
Publikováno v:
Journal of Synchrotron Radiation, Vol 29, Iss 5, Pp 1141-1151 (2022)
Serial synchrotron crystallography enables the study of protein structures under physiological temperature and reduced radiation damage by collection of data from thousands of crystals. The Structural Biology Center at Sector 19 of the Advanced Photo
Externí odkaz:
https://doaj.org/article/73d049967fd442e49c02f129554585bf
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
Autor:
Jose M. Martin-Garcia, Sabine Botha, Hao Hu, Rebecca Jernigan, Albert Castellví, Stella Lisova, Fernando Gil, Barbara Calisto, Isidro Crespo, Shatabdi Roy-Chowdhury, Alice Grieco, Gihan Ketawala, Uwe Weierstall, John Spence, Petra Fromme, Nadia Zatsepin, Dirk Roeland Boer, Xavi Carpena
Publikováno v:
Journal of Synchrotron Radiation, Vol 29, Iss 3, Pp 896-907 (2022)
The increase in successful adaptations of serial crystallography at synchrotron radiation sources continues. To date, the number of serial synchrotron crystallography (SSX) experiments has grown exponentially, with over 40 experiments reported so far
Externí odkaz:
https://doaj.org/article/bd920fee84a048b9b7eb3823938dba7e