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Articles by Florian Dworkowski
Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography - Nature Communications
Abstract Microbial rhodopsins form a diverse family of light-sensitive seven-transmembrane helix retinal proteins that function as active proton or ion pumps, passive light-gated ion channels, and photosensors.
Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate - Nature Communications
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Abstract Time-resolved serial crystallography at X-ray Free Electron Lasers offers the opportunity to observe ultrafast photochemical reactions at the atomic level. The technique has yielded exciting molecular insights into various biological processes including light sensing and photochemical energy conversion.
By Quentin Bertrand, Przemyslaw Nogly, Eriko Nango, Antonia Furrer, Florian Dworkowski, Per Börjesson, Giorgia Ortolani, Chia-Ying Huang, Michal W. Kepa, Dmitry Ozerov, Valerie Panneels, Kensuke Tono, Philip Johnson, Gregor Knopp, Claudio Cirelli, Christopher Milne, Gebhard Schertler, So Iwata, Richard Neutze, Tobias Weinert
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Nature
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Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography - Nature Chemistry
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Abstract Charge-transfer reactions in proteins are important for life, such as in photolyases which repair DNA, but the role of structural dynamics remains unclear. Here, using femtosecond X-ray crystallography, we report the structural changes that take place while electrons transfer along a chain of four conserved tryptophans in the Drosophila melanogaster (6-4) photolyase.
By Andrea Cellini, Madan Kumar Shankar, Amke Nimmrich, Leigh Hunt, Leonardo Monrroy, Emma V. Beale, Melissa Carrillo, Tek Narsingh Malla, Piotr Maj, Lidija Vrhovac, Florian Dworkowski, Claudio Cirelli, Philip Johnson, Dmitry Ozerov, Emina A. Stojković, Leif Hammarström, Camila Bacellar, Jörg Standfuss, Michał Maj, Marius Schmidt, Tobias Weinert, Janne A. Ihalainen
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Nature
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A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers - Nature Communications
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Abstract Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced.
By Maximilian Wranik, Quentin Bertrand, Tobias Weinert, Antonia Furrer, Hannah Glover Verified, Melissa Carrillo, Dmitry Ozerov, Claudio Cirelli, Philip Johnson, Florian Dworkowski, John Beale, Li Gao, Oliver Thorn-Seshold, Camila Bacellar, Michel O. Steinmetz, Christopher Milne, Michal W. Kepa, Emma V. Beale, Kristina Krauskopf
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Nature
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Watching the release of a photopharmacological drug from tubulin using time-resolved serial crystallography - Nature Communications
Abstract The binding and release of ligands from their protein targets is central to fundamental biological processes as well as to drug discovery. Photopharmacology introduces chemical triggers that allow the changing of ligand affinities and thus biological activity by light. Insight into the molecular mechanisms of photopharmacology is largely missing because the relevant transitions during the light-triggered reaction cannot be resolved by conventional structural biology.
Femtosecond-to-millisecond structural changes in a light-driven sodium pump
Abstract Light-driven sodium pumps actively transport small cations across cellular membranes1. These pumps are used by microorganisms to convert light into membrane potential and have become useful optogenetic tools with applications in neuroscience. Although the resting state structures of the prototypical sodium pump Krokinobacter eikastus rhodopsin 2 (KR2) have been solved2,3, it is unclear how structural alterations over time allow sodium to be translocated against a concentration gradient.
A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans
A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases from Streptomyces lividans Dye decolourising peroxidases (DyPs) are oxidative haem containing enzymes that can oxidise organic substrates by first reacting with hydrogen peroxide. Herein, we have focused on two DyP homologs, DtpAa and DtpA, from the soil-dwelling bacterium Streptomyces lividans.
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography
Research Article Tobias Weinert1,*, Petr Skopintsev1,†, Daniel James1,†, Florian Dworkowski2, Ezequiel Panepucci2, Demet Kekilli1, Antonia Furrer1, Steffen Brünle1, Sandra Mous3, Dmitry Ozerov4, Przemyslaw Nogly3, Meitian Wang2, Jörg Standfuss1 1Division of Biology and Chemistry–Laboratory for Biomolecular Research, Paul Scherrer Institut, 5232 Villigen, Switzerland. 2Macromolecular Crystallography, Swiss Light Source, Paul Scherrer Institut, 5232 Villigen PSI, Switzerland.
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