Zobrazeno 1 - 10
of 31
pro vyhledávání: '"E.L. Baxter"'
Autor:
Christopher O. Barnes, Aina E. Cohen, J. Song, E.L. Baxter, Nicholas K. Sauter, S.M. Soltis, Avram J. Holmes, Veeranagu Nagarajan, Jinwoo Ahn, Guowu Lin, Yijen L. Wu, Aaron S. Brewster, Guillermo Calero
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 19
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America
Significance While cellular dNTPases display broad activity toward dNTPs (e.g., SAMHD1), Escherichia coli (Ec)-dGTPase is the only known enzyme that specifically hydrolyzes dGTP. Here, we present methods for highly efficient, fixed-target X-ray free-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdf2f8be4137e7066f378ec0039dbbd8
https://escholarship.org/uc/item/4v75c32n
https://escholarship.org/uc/item/4v75c32n
Akademický článek
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Autor:
Aaron S. Brewster, Hilary P. Stevenson, E.L. Baxter, Xiaofeng Fu, Elena G. Kovaleva, Christopher O. Barnes, Daniel P. DePonte, Guillermo Calero, Aina E. Cohen
Publikováno v:
Archives of Biochemistry and Biophysics. 602:61-68
Serial femtosecond crystallography (SFX) employing high-intensity X-ray free-electron laser (XFEL) sources has enabled structural studies on microcrystalline protein samples at non-cryogenic temperatures. However, the identification and optimization
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
Autor:
Guillermo Calero, J. Song, E.L. Baxter, Nagarajan, Avram J. Holmes, Nicholas K. Sauter, Aaron S. Brewster, M. Soltis, Guowu Lin, Yang Wu, Adam E. Cohen, Christopher O. Barnes, Jinwoo Ahn
Deoxynucleotide triphosphate triphosphyohydrolyases (dNTPases) play a critical role in cellular survival and DNA replication through the proper maintenance of cellular dNTP pools by hydrolyzing dNTPs into deoxynucleosides and inorganic triphosphate (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::684e7138a8e8d800d3b1c818a756cd7e
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
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
X-ray free-electron lasers (XFELs) promise to enable the col
Autor:
Mohamed Ibrahim, Aina E. Cohen, William I. Weis, S.M. Soltis, Guillermo Calero, J. Song, E.L. Baxter, Axel T. Brunger, Jan Kern, Artem Y. Lyubimov, Andrew C. Kruse, William F. DeGrado, Roberto Alonso-Mori, Athina Zouni, Tom T. Caradoc-Davies, Brian K. Kobilka, Christopher A. Bonagura, Winnie Brehmer, Karl M. Larsson, Ruchira Chatterjee, S.E. McPhillips, Aashish Manglik, Yingssu Tsai, Erik Norgren, Heinrik T. Lemke, James S. Fraser, Jessica L. Thomaston, Vittal K. Yachandra, Junko Yano, Christopher O. Barnes, Rahel A. Woldeyes, Siew S. Pang, Laura Aguila
Publikováno v:
Baxter, EL; Aguila, L; Alonso-Mori, R; Barnes, CO; Bonagura, CA; Brehmer, W; et al.(2016). High-density grids for efficient data collection from multiple crystals. Acta Crystallographica Section D: Structural Biology, 72(1), 2-11. doi: 10.1107/S2059798315020847. UCSF: Retrieved from: http://www.escholarship.org/uc/item/6bt9p8m5
Acta crystallographica. Section D, Structural biology, vol 72, iss Pt 1
Acta Crystallographica. Section D, Structural Biology
Acta crystallographica. Section D, Structural biology, vol 72, iss Pt 1
Acta Crystallographica. Section D, Structural Biology
A high-density sample mount has been developed for efficient goniometer-based sample delivery at synchrotron and XFEL sources.
Higher throughput methods to mount and collect data from multiple small and radiation-sensitive crystals are important
Higher throughput methods to mount and collect data from multiple small and radiation-sensitive crystals are important
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0cb879cbc7396fe13c68166cc5709ee
http://www.escholarship.org/uc/item/6bt9p8m5
http://www.escholarship.org/uc/item/6bt9p8m5
Publikováno v:
Proceedings of the National Academy of Sciences. 108:5266-5271
MitoNEET is a recently identified drug target for a commonly prescribed diabetes drug, Pioglitazone. It belongs to a previously uncharacterized ancient family of proteins for which the hallmark is the presence of a unique 39 amino acid CDGSH domain.
Autor:
Axel T. Brunger, S. Michael Soltis, Aina E. Cohen, Ana Gonzalez, Monarin Uervirojnangkoorn, Lillian R. Kenner, Henry van den Bedem, Roberto Alonso-Mori, Matthew Warkentin, James S. Fraser, J. Song, E.L. Baxter, Henrik T. Lemke, Nicholas K. Sauter, Michael C. Thompson, Rahel A. Woldeyes, Andrew H. Van Benschoten, James M. Holton, S.E. McPhillips, Daniel A. Keedy, Aaron S. Brewster, Robert E. Thorne, Jesse B. Hopkins, William I. Weis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7536c7314a8681502a3fae61c60a61f
https://doi.org/10.7554/elife.07574.055
https://doi.org/10.7554/elife.07574.055
Autor:
Jesse B. Hopkins, Robert E. Thorne, Rahel A. Woldeyes, Michael C. Thompson, Ana Gonzalez, Axel T. Brunger, Andrew H. Van Benschoten, Nicholas K. Sauter, Monarin Uervirojnangkoorn, Scott E. McPhillps, Lillian R. Kenner, James M. Holton, Roberto Alonso-Mori, Henrik T. Lemke, S. Michael Soltis, Daniel A. Keedy, William I. Weis, Aina E. Cohen, Henry van den Bedem, Aaron S. Brewster, Matthew Warkentin, James S. Fraser, J. Song, E.L. Baxter
Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e61d56787b387070c9f8965911e7543
https://doi.org/10.1101/016733
https://doi.org/10.1101/016733