Goniometer-based femtosecond X-ray diffraction of mutant 30S ribosomal subunit crystals

Autor: E. Han Dao, Raymond G. Sierra, Hartawan Laksmono, Henrik T. Lemke, Roberto Alonso-Mori, Aaron Coey, Kevin Larsen, Elizabeth L. Baxter, Aina E. Cohen, S. Michael Soltis, Hasan DeMirci

Publikováno v: Structural Dynamics, Vol 2, Iss 4, Pp 041706-041706-10 (2015)

In this work, we collected radiation-damage-free data from a set of cryo-cooled crystals for a novel 30S ribosomal subunit mutant using goniometer-based femtosecond crystallography. Crystal quality assessment for these samples was conducted at the X-

Externí odkaz: https://doaj.org/article/3523372e8436431785b805c74f048bea

Crystal structure of the pristine peroxidase ferryl center and its relevance to proton-coupled electron transfer

Autor: Yergalem T. Meharenna, S. Michael Soltis, S.E. McPhillips, J. Song, E.L. Baxter, Georges Chreifi, Aina E. Cohen, Tzanko Doukov, Thomas L. Poulos

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, vol 113, iss 5

The reaction of peroxides with peroxidases oxidizes the heme iron from Fe(III) to Fe(IV)=O and a porphyrin or aromatic side chain to a cationic radical. X-ray-generated hydrated electrons rapidly reduce Fe(IV), thereby requiring very short exposures

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09e90fd8b5d21b1bf555234dd43988c1
https://doi.org/10.1073/pnas.1521664113

Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array

Autor: James M. Berger, E.L. Baxter, Thomas D. Murray, Ismail Emre Araci, Oliver B. Zeldin, Nicholas K. Sauter, Axel T. Brunger, S. Michael Soltis, Aina E. Cohen, Antoine Koehl, Monarin Uervirojnangkoorn, Aaron S. Brewster, Artem Y. Lyubimov

Publikováno v: Lyubimov, AY; Murray, TD; Koehl, A; Araci, IE; Uervirojnangkoorn, M; Zeldin, OB; et al.(2015). Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array. Acta Crystallographica Section D: Biological Crystallography, 71, 928-940. doi: 10.1107/S1399004715002308. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/44p6q103
Acta crystallographica. Section D, Biological crystallography, vol 71, iss Pt 4
Acta Crystallographica Section D: Biological Crystallography

A microfluidic platform has been developed for the capture and X-ray analysis of protein microcrystals, affording a means to improve the efficiency of XFEL and synchrotron experiments.
X-ray free-electron lasers (XFELs) promise to enable the col

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c98d84b32463ef3b25cb84b67940bb9
https://doi.org/10.1107/s1399004715002308

Use of transmission electron microscopy to identify nanocrystals of challenging protein targets

Autor: Monica Calero, Aina E. Cohen, Christopher O. Barnes, Irimpan I. Mathews, Guowu Lin, James F. Conway, Chaitan Khosla, Ted M. Ross, Hilary P. Stevenson, Alexander M. Makhov, Hugo Santamaria, Guillermo Calero, Andrea L. Edwards, Oliver B. Zeldin, S. Michael Soltis, Veeranagu Nagarajan

Publikováno v: Proceedings of the National Academy of Sciences. 111:8470-8475

The current practice for identifying crystal hits for X-ray crystallography relies on optical microscopy techniques that are limited to detecting crystals no smaller than 5 μm. Because of these limitations, nanometer-sized protein crystals cannot be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3959999aa0d1745b76498efbc2f029c1
https://doi.org/10.1073/pnas.1400240111

Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori

Autor: Hartmut Luecke, Keith Munson, S. Michael Soltis, Chiung-Kuang Chen, George Sachs, Reginald McNulty, David Strugatsky

Publikováno v: Nature
Nature, vol 493, iss 7431

Half the world's population is chronically infected with Helicobacter pylori, causing gastritis, gastric ulcers and an increased incidence of gastric adenocarcinoma. Its proton-gated inner-membrane urea channel, HpUreI, is essential for survival in t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73f121dad482b05e5bd9daa076c98413
http://europepmc.org/articles/PMC3974264