Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Yingssu Tsai"'
Autor:
Yingssu Tsai, Michael R Sawaya, Gordon C Cannon, Fei Cai, Eric B Williams, Sabine Heinhorst, Cheryl A Kerfeld, Todd O Yeates
Publikováno v:
PLoS Biology, Vol 5, Iss 6, p e144 (2007)
The carboxysome is a bacterial organelle that functions to enhance the efficiency of CO2 fixation by encapsulating the enzymes ribulose bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase. The outer shell of the carboxysome is reminis
Externí odkaz:
https://doaj.org/article/a9e7042d407c48f1adf5a582255a25b8
Autor:
Ana Gonzalez, Daniel Herschlag, Fanny Sunden, Jason P. Schwans, Benjamin J. Lengerich, Yingssu Tsai, Sharon Hammes-Schiffer, Philip Hanoian
Publikováno v:
Biochemistry
The positioning of catalytic groups within proteins plays an important role in enzyme catalysis, and here we investigate the positioning of the general base in the enzyme ketosteroid isomerase (KSI). The oxygen atoms of Asp38, the general base in KSI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c09348c0461cee6b5b6ef7be258c920f
http://europepmc.org/articles/PMC4004248
http://europepmc.org/articles/PMC4004248
Publikováno v:
Biochemistry. 52:7840-7855
Within the idiosyncratic enzyme active-site environment, side chain and ligand pKa values can be profoundly perturbed relative to their values in aqueous solution. Whereas structural inspection of systems has often attributed perturbed pKa values to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65b71b9e703cc742776706d080eb0788
https://doi.org/10.1021/bi401083b
https://doi.org/10.1021/bi401083b
Autor:
Daniel Herschlag, Yingssu Tsai, Jonathan K. Lassila, Ana Gonzalez, Jason P. Schwans, Fanny Sunden
Publikováno v:
Proceedings of the National Academy of Sciences. 110:11308-11313
Although the cation–pi pair, formed between a side chain or substrate cation and the negative electrostatic potential of a pi system on the face of an aromatic ring, has been widely discussed and has been shown to be important in protein structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::212196d9c9cc7f63322955308e708fd3
https://doi.org/10.1073/pnas.1206710110
https://doi.org/10.1073/pnas.1206710110
AutoDrug: fully automated macromolecular crystallography workflows for fragment-based drug discovery
Autor:
Britt Hedman, Bertram Ludaescher, Ana Gonzalez, Michael D. Feese, S. Michael Soltis, S.E. McPhillips, Yingssu Tsai, Aina E. Cohen, Timothy M. McPhillips, Keith O. Hodgson, David A. Bushnell, Daniel Zinn, C. David Stout, Theresa Tiefenbrunn
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 69:796-803
AutoDrug is software based upon the scientific workflow paradigm that integrates the Stanford Synchrotron Radiation Lightsource macromolecular crystallography beamlines and third-party processing software to automate the crystallography steps of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e8633781a4f7d07f2f8c07e9a6ed588
https://doi.org/10.1107/s0907444913001984
https://doi.org/10.1107/s0907444913001984
Publikováno v:
Journal of the American Chemical Society. 138(24)
Prior site-directed mutagenesis studies in bacterial ketosteroid isomerase (KSI) reported that substitution of both oxyanion hole hydrogen bond donors give a 105–108 fold rate reduction suggesting that the oxyanion hole may provide the major contri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f05f7c14e38c5f1c146773469a8e3af7
https://pubmed.ncbi.nlm.nih.gov/22053826
https://pubmed.ncbi.nlm.nih.gov/22053826
Autor:
Anthony Kuczewski, Alexei S. Soares, Jan Kern, Monarin Uervirojnangkoorn, Guangye Han, Silke Nelsen, S. Michael Soltis, Michael C. Browne, José Fernando Ruggiero Bachega, Nicholas K. Sauter, Brent L. Eaton, Mohamed Ibrahim, Diling Zhu, Heng Song, Richard G. Stearns, Martin Bommer, Sammy S. Datwani, Carrie M. Wilmot, Lucien P. Ghislain, Athina Zouni, Eunsun Cho, Yingssu Tsai, William M. McClintock, Stuart Myers, Matthew L. Cowan, Roberto Alonso-Mori, Lars Majlof, Annie Heroux, Aina E. Cohen, Victor L. Davidson, Marc Allaire, Allen M. Orville, Babak Andi, Joe Olechno, Yiping Feng, Erik T. Yukl, Rakhi Agarwal, Julia Hellmich, Johan Hattne, Ruchira Chatterjee, Henrik T. Lemke, Richard N. Ellson, Jim Defever, Christian G. Roessler, Vittal K. Yachandra, Junko Yano, Rosalie Tran, Pinghua Liu, Aaron S. Brewster, James M. Glownia
Publikováno v:
Structure (London, England : 1993), vol 24, iss 4
Roessler, CG; Agarwal, R; Allaire, M; Alonso-Mori, R; Andi, B; Bachega, JFR; et al.(2016). Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography. Structure, 24(4), 631-640. doi: 10.1016/j.str.2016.02.007. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/873254c1
Roessler, CG; Agarwal, R; Allaire, M; Alonso-Mori, R; Andi, B; Bachega, JFR; et al.(2016). Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography. Structure, 24(4), 631-640. doi: 10.1016/j.str.2016.02.007. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/873254c1
© 2016 Elsevier Ltd. All rights reserved. X-ray free-electron lasers (XFELs) provide very intense X-ray pulses suitable for macromolecular crystallography. Each X-ray pulse typically lasts for tens of femtoseconds and the interval between pulses is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a9f62a0e0836ff33da0b6a638974346
https://escholarship.org/uc/item/873254c1
https://escholarship.org/uc/item/873254c1
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:
Journal of the American Chemical Society. 133:20052-20055
Prior site-directed mutagenesis studies in bacterial ketosteroid isomerase (KSI) reported that substitution of both oxyanion hole hydrogen bond donors gives a 10(5)- to 10(8)-fold rate reduction, suggesting that the oxyanion hole may provide the majo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::935702953aad514f8d948d045233dc74
https://doi.org/10.1021/ja208050t
https://doi.org/10.1021/ja208050t
Publikováno v:
Biochemistry. 57:2176-2176
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7725cb3767d0b3e81a3a2a0f48911f83
https://doi.org/10.1021/acs.biochem.8b00246
https://doi.org/10.1021/acs.biochem.8b00246