Dr. Tobias Weinert

Curriculum Vitae

Serial crystallography and the dynamic nature of proteins


As a PI at LBR i am actively developing methods for time resolved serial crystallography at synchrotrons and free electron lasers. Bringing methods developed for free electron lasers to the synchrotron will dramatically widen the scope of time resolved, dynamic studies on protein molecules. Laser induced activation of conformational dynamics allows us to precisely trigger these dynamical processes. Precise triggers are the key to observe structural changes with atomic spatial precision and high temporal resolution by using time resolved serial crystallography. I am currently establishing a research program aiming to study targets that do not have intrinsic light switches.

As a scientist at LBR i am supporting serial crystallography activities at SLS as well as SwissFEL for all groups. I am the responsible scientist for the serial crystallography setup at SLS and am experienced in processing of serial crystallographic data.

• Full List on Google Scholar

• CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain. Aher A, Kok M, Sharma A, Rai A, Olieric N, Rodriguez-Garcia R, Katrukha EA, Weinert T, Olieric V, Kapitein LC, Steinmetz MO, Dogterom M, Akhmanova A
  DEVELOPMENTAL CELL 46, 40 (2018).
• Crystal structure of rhodopsin in complex with a mini-G o sheds light on the principles of G protein selectivity Tsai C, Pamula F, Nehmé R, Mühle J, Weinert T, Flock T, Nogly P, Edwards Patricia C, Carpenter B, Gruhl T, Ma P, Deupi X, Standfuss J, Tate Christopher G, Schertler Gebhard FX
  Science Advances 4, eaat7052 (2018).
  DOI: 10.1126/sciadv.aat7052
• In situ serial crystallography for rapid de novo membrane protein structure determination. Huang CY, Olieric V, Howe N, Warshamanage R, Weinert T, Panepucci E, Vogeley L, Basu S, Diederichs K, Caffrey M, Wang M
  Communications Biology 1, 124 (2018).
  DOI: 10.1038/S42003-018-0123-6
• Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser Nogly P, Weinert T, James D, Carbajo S, Ozerov D, Furrer A, Gashi D, Borin V, Skopintsev P, Jaeger K, Nass K, Båth P, Bosman R, Koglin J, Seaberg M, Lane T, Kekilli D, Brünle S, Tanaka T, Wu W, Milne C, White T, Barty A, Weierstall U, Panneels V, Nango E, Iwata S, Hunter M, Schapiro I, Schertler G, Neutze R, Standfuss J
  SCIENCE 361, 145 (2018).
  DOI: 10.1126/science.aat0094

• DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum. Jiang S, Wang L, Huang M, Jia Z, Weinert T, Warkentin E, Liu C, Song X, Zhang H, Witt J, Qiu L, Peng G, Song L
  Frontiers in Immunology 8, 1607 (2017).
• Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation. Vercellino I, Rezabkova L, Olieric V, Polyhach Y, Weinert T, Kammerer RA, Jeschke G, Korkhov VM
  PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 114, E9821 (2017).
  DOI: 10.1073/PNAS.1712621114
• Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons Weinert T, Olieric N, Cheng R, Brünle S, James D, Ozerov D, Gashi D, Vera L, Marsh M, Jaeger K, Dworkowski F, Panepucci E, Basu S, Skopintsev P, Doré Andrew S, Geng T, Cooke Robert M, Liang M, Prota Andrea E, Panneels V, Nogly P, Ermler U, Schertler G, Hennig M, Steinmetz Michel O, Wang M, Standfuss J
  NATURE COMMUNICATIONS 8, 542 (2017).
  DOI: 10.1038/s41467-017-00630-4
• Structure of the Full-length VEGFR-1 Extracellular Domain in Complex with VEGF-A. Markovic-Mueller S, Stuttfeld E, Asthana M, Weinert T, Bliven S, Goldie KN, Kisko K, Capitani G, Ballmer-Hofer K
  STRUCTURE 25, 341 (2017).
  DOI: 10.1016/J.STR.2016.12.012

• Data-collection strategy for challenging native SAD phasing Olieric V, Weinert T, Finke Aaron D, Anders C, Li D, Olieric N, Borca Camelia N, Steinmetz Michel O, Caffrey M, Jinek M, Wang M
  ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72, 421 (2016).
  DOI: 10.1107/S2059798315024110
• In meso in situ In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures Huang ChiaYing, Olieric Vincent, Ma Pikyee, Howe Nicole, Vogeley Lutz, Liu Xiangyu, Warshamanage Rangana, Weinert Tobias, Panepucci Ezequiel, Kobilka Brian, Diederichs Kay, Wang Meitian, Caffrey Martin
  ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72, 93-112 (2016).
  DOI: 10.1107/S2059798315021683
• In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures. Huang CY, Olieric V, Ma P, Howe N, Vogeley L, Liu X, Warshamanage R, Weinert T, Panepucci E, Kobilka B, Diederichs K, Wang M, Caffrey M
  ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 72, 93 (2016).
  DOI: 10.1107/S2059798315021683

• Fast native-SAD phasing for routine macromolecular structure determination Weinert Tobias, Olieric Vincent, Waltersperger Sandro, Panepucci Ezequiel, Chen Lirong, Zhang Hua, Zhou Dayong, Rose John, Ebihara Akio, Kuramitsu Seiki, Li Dianfan, Howe Nicole, Schnapp Gisela, Pautsch Alexander, Bargsten Katja, Prota Andrea E, Surana Parag, Kottur Jithesh, Nair Deepak T, Basilico Federica, Cecatiello Valentina, Pasqualato Sebastiano, Boland Andreas, Weichenrieder Oliver, Wang Bi-Cheng, Steinmetz Michel O, Caffrey Martin, Wang Meitian
  NATURE METHODS 12, 131-U163 (2015).
  DOI: 10.1038/nmeth.3211
• Fast native-SAD phasing for routine macromolecular structure determination (vol 12, pg 131, 2015) Weinert Tobias, Olieric Vincent, Waltersperger Sandro, Panepucci Ezequiel, Chen Lirong, Zhang Hua, Zhou Dayong, Rose John, Ebihara Akio, Kuramitsu Seiki, Li Dianfan, Howe Nicole, Schnapp Gisela, Pautsch Alexander, Bargsten Katja, Prota Andrea E, Surana Parag, Kottur Jithesh, Nair Deepak T, Basilico Federica, Cecatiello Valentina, Pasqualato Sebastiano, Boland Andreas, Weichenrieder Oliver, Wang BiCheng, Steinmetz Michel O, Caffrey Martin, Wang Meitian
  NATURE METHODS 12, 692-692 (2015).
• PRIGo: a new multi-axis goniometer for macromolecular crystallography Waltersperger Sandro, Olieric Vincent, Pradervand Claude, Glettig Wayne, Salathe Marco, Fuchs Martin R, Curtin Adrian, Wang Xiaoqiang, Ebner Simon, Panepucci Ezequiel, Weinert Tobias, Schulze-Briese Clemens, Wang Meitian
  JOURNAL OF SYNCHROTRON RADIATION 22, 895-900 (2015).
  DOI: 10.1107/S1600577515005354
• Structural basis of enzymatic benzene ring reduction Weinert Tobias, Huwiler Simona G, Kung Johannes W, Weidenweber Sina, Hellwig Petra, Staerk HansJoachim, Biskup Till, Weber Stefan, Cotelesage Julien J H, George Graham N, Ermler Ulrich, Boll Matthias
  NATURE CHEMICAL BIOLOGY 11, 586-U123 (2015).
  DOI: 10.1038/NCHEMBIO.1849
• Structural basis of enzymatic benzene ring reduction (vol 11, pg 586, 2015) Weinert Tobias, Huwiler Simona G, Kung Johannes W, Weidenweber Sina, Hellwig Petra, Staerk HansJoachim, Biskup Till, Weber Stefan, Cotelesage Julien J H, George Graham N, Ermler Ulrich, Boll Matthias
  NATURE CHEMICAL BIOLOGY 11, 741-741 (2015).
• Structural basis of enzymatic benzene ring reduction (vol 18, pg 586, 2015) Weinert Tobias, Huwiler Simona G, Kung Johannes W, Weidenweber Sina, Hellwig Petra, Staerk HansJoachim, Biskup Till, Weber Stefan, Cotelesage Julien J H, George Graham N, Ermler Ulrich, Boll Matthias
  NATURE CHEMICAL BIOLOGY 11, 815-815 (2015).

• Benzoyl-CoA Epoxidase of Azoarcus evansii Weinert T, Rather-Adler LJ, Bill E, Fuchs G, Ermler U
  Encyclopedia of Inorganic and Bioinorganic Chemistry 1-13, (2013).
  DOI: 10.1002/9781119951438.eibc2170

• Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically Shima Seigo, Krueger Martin, Weinert Tobias, Demmer Ulrike, Kahnt Joerg, Thauer Rudolf K, Ermler Ulrich
  NATURE 481, 98-101 (2012).
  DOI: 10.1038/nature10663

• Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB Rather LJ, Weinert T, Demmer U, Bill E, Ismail W, Fuchs G, Ermler U
  JOURNAL OF BIOLOGICAL CHEMISTRY 286, 29241 (2011).
  DOI: 10.1074/jbc.M111.236893