Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Eike C. Schulz"'
Autor:
Pedram Mehrabi, Sihyun Sung, David von Stetten, Andreas Prester, Caitlin E. Hatton, Stephan Kleine-Döpke, Alexander Berkes, Gargi Gore, Jan-Philipp Leimkohl, Hendrik Schikora, Martin Kollewe, Holger Rohde, Matthias Wilmanns, Friedjof Tellkamp, Eike C. Schulz
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-9 (2023)
Abstract We introduce the spitrobot, a protein crystal plunger, enabling reaction quenching via cryo-trapping with a time-resolution in the millisecond range. Protein crystals are mounted on canonical micromeshes on an electropneumatic piston, where
Externí odkaz:
https://doaj.org/article/134dae128c544ebf932ba2feffdff61b
Autor:
Robert Bücker, Pascal Hogan-Lamarre, Pedram Mehrabi, Eike C. Schulz, Lindsey A. Bultema, Yaroslav Gevorkov, Wolfgang Brehm, Oleksandr Yefanov, Dominik Oberthür, Günther H. Kassier, R. J. Dwayne Miller
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
For conventional three-dimensional microcrystal electron diffraction (3D ED/MicroED), a crystal is slowly rotated under an electron beam, leading to inevitable accumulation of radiation damage during data collection. In this work, the authors present
Externí odkaz:
https://doaj.org/article/dbd92ddaa279416f9b79929ff4e04966
Autor:
Pedram Mehrabi, Eike C. Schulz
Publikováno v:
Advanced Methods in Structural Biology
Methods in Molecular Biology ISBN: 9781071631461
Methods in Molecular Biology ISBN: 9781071631461
Time-resolved serial crystallography is an emerging method to elucidate the structure-function relationship of biomolecular systems at up to atomic resolution. However, to make this demanding method a success, a number of experimental requirements ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe50c8c68477f7a0a31d7d124d8411de
https://hdl.handle.net/21.11116/0000-000D-10F5-C21.11116/0000-000D-10F7-A
https://hdl.handle.net/21.11116/0000-000D-10F5-C21.11116/0000-000D-10F7-A
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
'Acta Crystallographica D ', vol: 78, pages: 14-29 (2022)
'Acta Crystallographica D ', vol: 78, pages: 14-29 (2022)
The key factors that should be considered during the planning and execution of a time-resolved crystallographic experiment are discussed, with a focus on time-resolved serial synchrotron crystallography.
With recent developments in X-ray sources
With recent developments in X-ray sources
Autor:
Pedram Mehrabi, Sihyun Sung, David von Stetten, Andreas Prester, Caitlin E. Hatton, Stephan Kleine-Döpke, Alexander Berkes, Gargi Gore, Jan-Philipp Leimkohl, Hendrik Schikora, Martin Kollewe, Holger Rohde, Matthias Wilmanns, Friedjof Tellkamp, Eike C. Schulz
We introduce the spitrobot, a protein crystal plunger, enabling reaction quenching via cryo-trapping with millisecond time-resolution. Canonical micromesh loops are mounted on an electropneumatic piston, reactions are initiated via the liquid applica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7b8e425cfdb80c3160946f8925bad484
https://doi.org/10.1101/2022.09.20.508674
https://doi.org/10.1101/2022.09.20.508674
Autor:
Pedram Mehrabi, Lars Redecke, David von Stetten, Eike C. Schulz, R. Schonherr, J. Boger, Ashley O. Kwok, R. J. Dwayne Miller, Brenna Norton-Baker, H. Schikora, Rachel W. Martin
Publikováno v:
Acta crystallographica / Section D 77(6), 820-834 (2021). doi:10.1107/S2059798321003855
Acta Crystallographica. Section D, Structural Biology
Acta Crystallographica Section D: Structural Biology
Acta Crystallographica. Section D, Structural Biology
Acta Crystallographica Section D: Structural Biology
Acta crystallographica / Section D 77(6), 820 - 834 (2021). doi:10.1107/S2059798321003855
Fixed-target serial crystallography has become an important method for the study of protein structure and dynamics at synchrotrons and X-ray free-electron
Fixed-target serial crystallography has become an important method for the study of protein structure and dynamics at synchrotrons and X-ray free-electron
Autor:
Arwen R. Pearson, H. Schikora, R. J. Dwayne Miller, Pedram Mehrabi, Jan Philipp Leimkohl, Robin L. Owen, Friedjof Tellkamp, Henrike M. Müller-Werkmeister, Ladislav Andricek, Sascha W. Epp, D.A. Sherrell, Jelena Ninkovic, Silvia Krivokuca, Eike C. Schulz
Publikováno v:
Journal of Synchrotron Radiation; Wiley-Blackwell on behalf of the IUCr
Journal of synchrotron radiation 27(2), 360-370 (2020). doi:10.1107/S1600577520000685
Journal of Synchrotron Radiation
Journal of synchrotron radiation 27(2), 360-370 (2020). doi:10.1107/S1600577520000685
Journal of Synchrotron Radiation
Journal of synchrotron radiation 27(2), 360 - 370 (2020). doi:10.1107/S1600577520000685
Serial synchrotron crystallography (SSX) is an emerging technique for static and time-resolved protein structure determination. Using specifically patterned
Serial synchrotron crystallography (SSX) is an emerging technique for static and time-resolved protein structure determination. Using specifically patterned
We present a new environmental enclosure for fixed-target, serial crystallography enabling full control of both the temperature and humidity. While maintaining the relative humidity to within a percent, this enclosure provides access to X-ray diffrac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01620859800ca195387e3c0373d319d2
https://doi.org/10.1101/2021.11.07.467596
https://doi.org/10.1101/2021.11.07.467596
Autor:
M. Schwinzer, Faisal Hammad Mekky Koua, Ashwin Chari, J. Lieske, Maria Garcia-Alai, Gleb Bourenkov, Russell J. Cox, Salah Awel, W. Ewert, Dušan Turk, Luca Gelisio, N. Werner, Hévila Brognaro, J. Pletzer-Zelgert, Juraj Knoska, Arwen R. Pearson, D. Melo, Matthias Rarey, Ilona Dunkel, Boris Krichel, Y. Gevorkov, A. Tolstikova, David von Stetten, Eike C. Schulz, Andrea Zaliani, Winfried Hinrichs, F. Trost, Helen M. Ginn, Xinyuanyuan Sun, Stephan Niebling, Holger Fleckenstein, Aleksandra Usenik, J. Wollenhaupt, Robin Schubert, Stephan Günther, Kristina Lorenzen, J. Boger, P. Reinke, Diana C. F. Monteiro, Bruno Alves Franca, Isabel Bento, Manfred S. Weiss, Ariana Peck, Dominik Oberthuer, Pedram Mehrabi, Pontus Fischer, Sebastian Günther, Jure Loboda, P. Lourdu Xavier, C. Schmidt, Christian Betzel, Huijong Han, N. Ullah, Philip Gribbon, Aida Rahmani Mashhour, Charlotte Uetrecht, Guillaume Pompidor, Christiane Ehrt, Christian G. Feiler, Saravanan Panneerselvam, Bernhard Ellinger, Christian M. Günther, Thomas J. Lane, Linlin Zhang, S. Meier, Tobias Beck, Henry N. Chapman, M. Domaracky, Sven Falke, Katarina Karničar, Markus Wolf, Cromarte Rogers, S. Saouane, Ivars Karpics, Rolf Hilgenfeld, Gisel E. Peña-Murillo, Vasundara Srinivasan, Alke Meents, Miriam Barthelmess, M. Galchenkova, B. Seychell, Beatriz Escudero-Pérez, Thomas A. White, Janine-Denise Kopicki, Joanna J. Zaitseva-Doyle, W. Brehm, M. Groessler, Brenna Norton-Baker, Frank Schlünzen, Chufeng Li, Henning Tidow, Maria Kuzikov, Andrea R. Beccari, Johanna Hakanpää, Henry Gieseler, Yaiza Fernández-García, Oleksandr Yefanov, Thomas R. Schneider, Anna Hänle, Jan Meyer, H. Andaleeb, V. Hennicke
Publikováno v:
Science (New York, N.y.)
Science 372 (6542): 642-646 (2021-05-07)
Science
Science / Science now 372(6542), 642-646 (2021). doi:10.1126/science.abf7945
Science 372 (6542): 642-646 (2021-05-07)
Science
Science / Science now 372(6542), 642-646 (2021). doi:10.1126/science.abf7945
A large-scale screen to target SARS-CoV-2 The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) genome is initially expressed as two large polyproteins. Its main protease, Mpro, is essential to yield functional viral proteins, making it a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a7f9ac410aabd144f9e9014ed83aff5
https://resolver.caltech.edu/CaltechAUTHORS:20201113-100151878
https://resolver.caltech.edu/CaltechAUTHORS:20201113-100151878
Autor:
Eike C. Schulz, Sana Azim, Jan-Philipp Leimkohl, Michiel B. de Kock, Günther Kassier, Friedjof Tellkamp, Niels de Jonge, Ernesto Rafael Osorio-Blanco, Sercan Keskin, Marcelo Calderón, R. J. Dwayne Miller, Josef Gonschior, Lindsey A. Bultema, Robert Bücker
Publikováno v:
Microscopy and Microanalysis
Liquid-phase transmission electron microscopy is a technique for simultaneous imaging of the structure and dynamics of specimens in a liquid environment. The conventional sample geometry consists of a liquid layer tightly sandwiched between two Si3N4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a904c6a189a5a6c8c9ac958fb382432a
https://hdl.handle.net/21.11116/0000-0008-0420-F21.11116/0000-0007-87FC-521.11116/0000-0007-87FF-2
https://hdl.handle.net/21.11116/0000-0008-0420-F21.11116/0000-0007-87FC-521.11116/0000-0007-87FF-2