S
Sadia Bari
Researcher at University of Hamburg
Publications - 81
Citations - 2172
Sadia Bari is an academic researcher from University of Hamburg. The author has contributed to research in topics: Ion & Ionization. The author has an hindex of 23, co-authored 72 publications receiving 1757 citations. Previous affiliations of Sadia Bari include Max Planck Society & University of Groningen.
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Journal ArticleDOI
Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser.
Christopher Kupitz,Shibom Basu,Ingo Grotjohann,Raimund Fromme,Nadia A. Zatsepin,Kimberly N. Rendek,Mark S. Hunter,Mark S. Hunter,Robert L. Shoeman,Thomas A. White,Dingjie Wang,Daniel James,Jay-How Yang,Danielle E. Cobb,Brenda Reeder,Raymond G. Sierra,Haiguang Liu,Anton Barty,Andrew Aquila,Daniel P. DePonte,Richard A. Kirian,Sadia Bari,Jesse J. Bergkamp,Kenneth R. Beyerlein,Michael J. Bogan,Carl Caleman,Tzu-Chiao Chao,Tzu-Chiao Chao,Chelsie E. Conrad,Katherine M. Davis,Holger Fleckenstein,Lorenzo Galli,Stefan P. Hau-Riege,Stephan Kassemeyer,Hartawan Laksmono,Mengning Liang,Lukas Lomb,Stefano Marchesini,Andrew V. Martin,Marc Messerschmidt,Despina Milathianaki,Karol Nass,Alexandra Ros,Shatabdi Roy-Chowdhury,Kevin Schmidt,M. Marvin Seibert,M. Marvin Seibert,Jan Steinbrener,Francesco Stellato,Lifen Yan,Chun Hong Yoon,Thomas A. Moore,Ana L. Moore,Yulia Pushkar,Garth J. Williams,Sébastien Boutet,R. Bruce Doak,Uwe Weierstall,Matthias Frank,Henry N. Chapman,John C. H. Spence,Petra Fromme +61 more
TL;DR: Time resolved experiments on PSII nano/microcrystals from Thermosynechococcus elongatus performed with the recently developed technique of serial femtosecond crystallography provide evidence that PSII undergoes significant conformational changes at the electron acceptor side and at the Mn4CaO5 core of the OEC.
Journal ArticleDOI
Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser.
David Arnlund,Linda C. Johansson,Cecilia Wickstrand,Anton Barty,Garth J. Williams,Erik Malmerberg,Jan Davidsson,Despina Milathianaki,Daniel P. DePonte,Robert L. Shoeman,Dingjie Wang,Daniel James,Gergely Katona,Sebastian Westenhoff,Thomas A. White,Andrew Aquila,Sadia Bari,Peter Berntsen,Michael J. Bogan,Tim Brandt van Driel,R. Bruce Doak,Kasper S. Kjær,Kasper S. Kjær,Matthias Frank,Raimund Fromme,Ingo Grotjohann,Robert Henning,Mark S. Hunter,Richard A. Kirian,Irina Kosheleva,Christopher Kupitz,Mengning Liang,Andrew V. Martin,Martin Nielsen,Marc Messerschmidt,M. Marvin Seibert,Jennie Sjöhamn,Francesco Stellato,Uwe Weierstall,Nadia A. Zatsepin,John C. H. Spence,Petra Fromme,Ilme Schlichting,Sébastien Boutet,Gerrit Groenhof,Henry N. Chapman,Richard Neutze +46 more
TL;DR: This work demonstrates an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein, providing direct structural evidence for a 'protein quake'.
Journal ArticleDOI
Megahertz serial crystallography
Max O. Wiedorn,Dominik Oberthür,Richard Bean,Robin Schubert,Robin Schubert,N. Werner,Brian Abbey,Martin Aepfelbacher,Luigi Adriano,A. Allahgholi,Nasser Al-Qudami,Jakob Andreasson,Jakob Andreasson,Jakob Andreasson,Steve Aplin,Salah Awel,Kartik Ayyer,Saša Bajt,Imrich Barák,Sadia Bari,Johan Bielecki,Sabine Botha,Djelloul Boukhelef,W. Brehm,Sandor Brockhauser,Sandor Brockhauser,Igor Cheviakov,Matthew A. Coleman,Francisco Cruz-Mazo,Cyril Danilevski,Connie Darmanin,R. Bruce Doak,M. Domaracky,Katerina Dörner,Yang Du,Hans Fangohr,Hans Fangohr,Holger Fleckenstein,Matthias Frank,Petra Fromme,Alfonso M. Gañán-Calvo,Y. Gevorkov,Klaus Giewekemeyer,Helen M. Ginn,Heinz Graafsma,Rita Graceffa,Dominic Greiffenberg,Lars Gumprecht,P. Gottlicher,Janos Hajdu,Janos Hajdu,Steffen Hauf,Michael Heymann,Susannah Holmes,Daniel A. Horke,Mark S. Hunter,Siegfried Imlau,Alexander Kaukher,Yoonhee Kim,A. Klyuev,Juraj Knoska,Bostjan Kobe,Manuela Kuhn,Christopher Kupitz,Jochen Küpper,Janine Mia Lahey-Rudolph,Torsten Laurus,Karoline Le Cong,Romain Letrun,P. Lourdu Xavier,Luis Maia,Filipe R. N. C. Maia,Filipe R. N. C. Maia,Valerio Mariani,Marc Messerschmidt,Markus Metz,Davide Mezza,Thomas Michelat,Grant Mills,Diana C. F. Monteiro,Andrew J. Morgan,Kerstin Mühlig,Anna Munke,Astrid Münnich,Julia Nette,Keith A. Nugent,Theresa Nuguid,Allen M. Orville,Suraj Pandey,Gisel Pena,Pablo Villanueva-Perez,J. Poehlsen,Gianpietro Previtali,Lars Redecke,Lars Redecke,Winnie Maria Riekehr,Holger Rohde,Adam Round,Tatiana Safenreiter,Iosifina Sarrou,Tokushi Sato,Marius Schmidt,Bernd Schmitt,R. Schonherr,Joachim Schulz,Jonas A. Sellberg,M. Marvin Seibert,Carolin Seuring,Megan L. Shelby,Robert L. Shoeman,M. Sikorski,Alessandro Silenzi,Claudiu A. Stan,Xintian Shi,Stephan Stern,Jola Sztuk-Dambietz,Janusz Szuba,Aleksandra Tolstikova,Martin Trebbin,Martin Trebbin,U. Trunk,Patrik Vagovic,Thomas Ve,Britta Weinhausen,Thomas A. White,Krzysztof Wrona,Chen Xu,Oleksandr Yefanov,Nadia A. Zatsepin,J. Zhang,Markus Perbandt,Adrian P. Mancuso,Christian Betzel,Christian Betzel,Henry N. Chapman,Anton Barty +135 more
TL;DR: It is demonstrated that high-quality and damage-free protein structures can be obtained with the currently available 1.1 MHz repetition rate pulses using lysozyme as a test case and furthermore a β-lactamase structure.
Journal ArticleDOI
Ion-induced biomolecular radiation damage: From isolated nucleobases to nucleobase clusters
Thomas Schlathölter,F. Alvarado,Sadia Bari,Aurelie Lecointre,Ronnie Hoekstra,Virgil Bernigaud,Bruno Manil,Jimmy Rangama,Bernd A. Huber +8 more
TL;DR: In this paper, the authors studied the interactions of keV ions with isolated nucleobases and with nucleobase clusters by means of coincidence time-of-flight spectrometry.
Journal ArticleDOI
Photodissociation of protonated leucine-enkephalin in the VUV range of 8-40 eV.
Sadia Bari,O. González-Magaña,G. Reitsma,Josephina Werner,Stefan Schippers,Ronnie Hoekstra,Thomas Schlathölter +6 more
TL;DR: For photon energies exceeding 10 eV a new dissociation scheme is identified in which photoabsorption leads to a fast loss of the tyrosine side chain, which leads to the formation of a residual peptide that is remarkably cold internally.