Dr. Tobias Weinert
5232 Villigen PSI
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.
CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain.
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
Science Advances 4, eaat7052 (2018).DOI: 10.1126/sciadv.aat7052
In situ serial crystallography for rapid de novo membrane protein structure determination.
Communications Biology 1, 124 (2018).DOI: 10.1038/S42003-018-0123-6
Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser
SCIENCE 361, 145 (2018).DOI: 10.1126/science.aat0094
DM9 Domain Containing Protein Functions As a Pattern Recognition Receptor with Broad Microbial Recognition Spectrum.
Frontiers in Immunology 8, 1607 (2017).
Role of the nucleotidyl cyclase helical domain in catalytically active dimer formation.
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
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.
STRUCTURE 25, 341 (2017).DOI: 10.1016/J.STR.2016.12.012
Data-collection strategy for challenging native SAD phasing
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
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.
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 72, 93 (2016).DOI: 10.1107/S2059798315021683
Fast native-SAD phasing for routine macromolecular structure determination
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)
NATURE METHODS 12, 692-692 (2015).
PRIGo: a new multi-axis goniometer for macromolecular crystallography
JOURNAL OF SYNCHROTRON RADIATION 22, 895-900 (2015).DOI: 10.1107/S1600577515005354
Structural basis of enzymatic benzene ring reduction
NATURE CHEMICAL BIOLOGY 11, 586-U123 (2015).DOI: 10.1038/NCHEMBIO.1849
Structural basis of enzymatic benzene ring reduction (vol 11, pg 586, 2015)
NATURE CHEMICAL BIOLOGY 11, 741-741 (2015).
Structural basis of enzymatic benzene ring reduction (vol 18, pg 586, 2015)
NATURE CHEMICAL BIOLOGY 11, 815-815 (2015).
Benzoyl-CoA Epoxidase of Azoarcus evansii
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
NATURE 481, 98-101 (2012).DOI: 10.1038/nature10663
Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB
JOURNAL OF BIOLOGICAL CHEMISTRY 286, 29241 (2011).DOI: 10.1074/jbc.M111.236893