BEGIN:VCALENDAR VERSION:2.0 PRODID:-//CERN//INDICO//EN BEGIN:VEVENT SUMMARY:Serial femtosecond crystallography of high-valent metal sites and protein radicals DTSTART;VALUE=DATE-TIME:20250923T084500Z DTEND;VALUE=DATE-TIME:20250923T091500Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1848@lindico453.srv.lu.se DESCRIPTION:Speakers: Martin Högbom (Stockholm University)\nHögbom\, M 1 \n\n1. Department of Biochemistry and Biophysics\, Stockholm University\, 10691 Stockholm\, Sweden.\n\nHigh resolution structure determination metho ds suffer from problems with radiation damage. This is particularly proble matic for radiation sensitive states such as high-valent metal sites and r adicals. From a chemical perspective this means that some of the most rele vant states for catalysis in many enzyme systems are inaccessible to stand ard structure determination regimes. \nIn close collaboration with scienti sts at the LCLS and the LBNL we utilize a conveyor-belt sample injector th at allows micrometer-sized crystals to be manipulated in various ways\, in cluding oxygen incubation for a defined period of time\, before exposure t o the free-electron laser X-ray beam [1]. This setup allows varying the ti me for intermediate trapping while the use of femtosecond XFEL crystallogr aphy eliminates the effect of X-ray photoreduction on obtained data. Simul taneous XES also allows in situ oxidation state determination of probed in termediates for metalloprotein systems. \nThis setup and its use to obtain high-resolution global geometric structures of high-valent intermediates will be discussed\, as well as our recent progress defining radiation unda maged structures of methane monooxygenase [2] and ribonucleotide reductase R2 proteins [3\,4] including the catalytic radical state [5].\n\n\nAcknow ledgments: This work was funded by the Knut and Alice Wallenberg Foundatio n\, the Swedish Research Council and the European Research Council (ERC).\ n\nReferences\n[1] F.D. Fuller et al. Nature Methods\, 14(4):443-449 (2017 )\n[2] Srinivas V. et al. J Am Chem Soc\, 142:14249-14266 (2020)\n[3] Srin ivas V. et al. Nature\, 563:416-420 (2018)\n[4] John J. et al. Elife\, 11: e79226 (2022)\n[5] Lebrette H. et al. Science\, 382:109-113 (2023)\n\nhttp s://lindico453.srv.lu.se/event/583/contributions/1848/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1848/ END:VEVENT BEGIN:VEVENT SUMMARY:Data analysis at MicroMAX DTSTART;VALUE=DATE-TIME:20250923T121000Z DTEND;VALUE=DATE-TIME:20250923T123000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1853@lindico453.srv.lu.se DESCRIPTION:Speakers: Cecilia Casadei (MAX IV Laboratory)\nThe rise of 4th generation sources\, including the MAX IV Laboratory 3 GeV ring\, has ena bled new possibilities to study dynamics using crystallography. The MicroM AX beamline is a new beamline focussed on providing optimal X-ray characte ristics for serial (SSX) and time-resolved (TR-SSX) crystallography at MAX IV [1]. The beamline emphasizes a flexible sample environment for standar d and bespoke experimental setups while also supporting high-throughput si ngle crystal data collections at the BioMAX beamline which has operated si nce 2017 [2]. \nThe MicroMAX user program opened in May 2024 and has perfo rmed experiments with SPINE-based fixed targets\, high-viscosity extrusion and microfluidics and single-crystal oscillation data collections. Sample handling and positioning is supported by the MD3-up micro diffractometer\ , Oxford cryojet\, and ISARA automated sample mounting platform (including crystallization plates). Time resolved techniques are enabled by a nanose cond pump laser (210-2600 nm)\, Celerotron X-ray chopper (0\,8-70% duty cy cle) and one of either an Eiger2 X 9M CdTe photon counting hybrid pixel de tector or Jungfrau 9M Si integrating hybrid pixel detector (on-loan from P SI). \nOptical elements allow for a beamline flux from 10^13 photons/s (0. 1% bandwidth double crystal monochromator) to more than 10^14 photons/s (1 % bandwidth multilayer monochromator) with an optimal 1x1 μm beam focus u sing beryllium lenses/K-B mirrors. Beamline controls are from within MXCuB E\, with additional live feedback and CrystFEL autoprocessing pipelines to provide immediate feedback and rapid map generation. Sample pre-character ization is supported by an offline laser and spectroscopy lab in the secon dary experimental hutch and dedicated sample environment and preparation l abs.\nHere we present the current status of MicroMAX beamline and recent d evelopments in sample preparation and data handling under a variety of exp erimental contexts. This work emphasizes the technical developments for a highly flexible TR-SSX end station in context of SSX/TR-SSX experiments al ready being conducted by the MicroMAX user community.\n\nMicroMAX is funde d by the Novo Nordisk Foundation under the grant number NNF17CC0030666.\n\ n[1] Gonzalez\, A.\, Krojer\, T.\, Nan\, J.\, Bjelcic\, M.\, Aggarwal\, S. \, Gorgisyan\, I.\, Milas\, M.\, Eguiraun\, M.\, Casadei\, C.\, Chenchiliy an\, M.\, Jurgilaitis\, A.\, Kroon\, D.\, Ahn\, B.\, Ekstrom\, J. C.\, Aur elius\, O.\, Lang\, D.\, Ursby\, T. & Thunnissen\, M. M. G. M. (2025). J. Synchrotron Rad. 32.\n[2] Shilova\, A.\, Lebrette\, H.\, Aurelius\, O.\, N an\, J.\, Welin\, M.\, Kovacic\, R.\, Ghosh\, S.\, Safari\, C.\, Friel\, R . J.\, Milas\, M.\, Matej\, Z.\, Högbom\, M.\, Brändén\, G.\, Kloos\, M .\, Shoeman\, R. L.\, Doak\, B.\, Ursby\, T.\, Håkansson\, M.\, Logan\, D . T. & Mueller U. (2020). J. Synchrotron Rad.\, 27\, 1095.\n\nhttps://lind ico453.srv.lu.se/event/583/contributions/1853/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1853/ END:VEVENT BEGIN:VEVENT SUMMARY:Sample delivery at MicroMAX DTSTART;VALUE=DATE-TIME:20250923T115000Z DTEND;VALUE=DATE-TIME:20250923T121000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1852@lindico453.srv.lu.se DESCRIPTION:Speakers: Dean Lang (MAX IV Laboratory)\nThe rise of 4th gener ation sources\, including the MAX IV Laboratory 3 GeV ring\, has enabled n ew possibilities to study dynamics using crystallography. The MicroMAX bea mline is a new beamline focussed on providing optimal X-ray characteristic s for serial (SSX) and time-resolved (TR-SSX) crystallography at MAX IV [1 ]. The beamline emphasizes a flexible sample environment for standard and bespoke experimental setups while also supporting high-throughput single c rystal data collections at the BioMAX beamline which has operated since 20 17 [2]. \nThe MicroMAX user program opened in May 2024 and has performed e xperiments with SPINE-based fixed targets\, high-viscosity extrusion and m icrofluidics and single-crystal oscillation data collections. Sample handl ing and positioning is supported by the MD3-up micro diffractometer\, Oxfo rd cryojet\, and ISARA automated sample mounting platform (including cryst allization plates). Time resolved techniques are enabled by a nanosecond p ump laser (210-2600 nm)\, Celerotron X-ray chopper (0\,8-70% duty cycle) a nd one of either an Eiger2 X 9M CdTe photon counting hybrid pixel detector or Jungfrau 9M Si integrating hybrid pixel detector (on-loan from PSI). \ nOptical elements allow for a beamline flux from 10^13 photons/s (0.1% ban dwidth double crystal monochromator) to more than 10^14 photons/s (1% band width multilayer monochromator) with an optimal 1x1 μm beam focus using b eryllium lenses/K-B mirrors. Beamline controls are from within MXCuBE\, wi th additional live feedback and CrystFEL autoprocessing pipelines to provi de immediate feedback and rapid map generation. Sample pre-characterizatio n is supported by an offline laser and spectroscopy lab in the secondary e xperimental hutch and dedicated sample environment and preparation labs.\n Here we present the current status of MicroMAX beamline and recent develop ments in sample preparation and data handling under a variety of experimen tal contexts. This work emphasizes the technical developments for a highly flexible TR-SSX end station in context of SSX/TR-SSX experiments already being conducted by the MicroMAX user community.\n\nMicroMAX is funded by t he Novo Nordisk Foundation under the grant number NNF17CC0030666.\n\n[1] G onzalez\, A.\, Krojer\, T.\, Nan\, J.\, Bjelcic\, M.\, Aggarwal\, S.\, Gor gisyan\, I.\, Milas\, M.\, Eguiraun\, M.\, Casadei\, C.\, Chenchiliyan\, M .\, Jurgilaitis\, A.\, Kroon\, D.\, Ahn\, B.\, Ekstrom\, J. C.\, Aurelius\ , O.\, Lang\, D.\, Ursby\, T. & Thunnissen\, M. M. G. M. (2025). J. Synchr otron Rad. 32.\n[2] Shilova\, A.\, Lebrette\, H.\, Aurelius\, O.\, Nan\, J .\, Welin\, M.\, Kovacic\, R.\, Ghosh\, S.\, Safari\, C.\, Friel\, R. J.\, Milas\, M.\, Matej\, Z.\, Högbom\, M.\, Brändén\, G.\, Kloos\, M.\, Sh oeman\, R. L.\, Doak\, B.\, Ursby\, T.\, Håkansson\, M.\, Logan\, D. T. & Mueller U. (2020). J. Synchrotron Rad.\, 27\, 1095.\n\nhttps://lindico453 .srv.lu.se/event/583/contributions/1852/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1852/ END:VEVENT BEGIN:VEVENT SUMMARY:MicroMAX - Overview DTSTART;VALUE=DATE-TIME:20250923T113000Z DTEND;VALUE=DATE-TIME:20250923T115000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1851@lindico453.srv.lu.se DESCRIPTION:Speakers: Jie Nan (MAX IV Laboratory)\nThe rise of 4th generat ion sources\, including the MAX IV Laboratory 3 GeV ring\, has enabled new possibilities to study dynamics using crystallography. The MicroMAX beaml ine is a new beamline focussed on providing optimal X-ray characteristics for serial (SSX) and time-resolved (TR-SSX) crystallography at MAX IV [1]. The beamline emphasizes a flexible sample environment for standard and be spoke experimental setups while also supporting high-throughput single cry stal data collections at the BioMAX beamline which has operated since 2017 [2]. \nThe MicroMAX user program opened in May 2024 and has performed exp eriments with SPINE-based fixed targets\, high-viscosity extrusion and mic rofluidics and single-crystal oscillation data collections. Sample handlin g and positioning is supported by the MD3-up micro diffractometer\, Oxford cryojet\, and ISARA automated sample mounting platform (including crystal lization plates). Time resolved techniques are enabled by a nanosecond pum p laser (210-2600 nm)\, Celerotron X-ray chopper (0\,8-70% duty cycle) and one of either an Eiger2 X 9M CdTe photon counting hybrid pixel detector o r Jungfrau 9M Si integrating hybrid pixel detector (on-loan from PSI). \nO ptical elements allow for a beamline flux from 10^13 photons/s (0.1% bandw idth double crystal monochromator) to more than 10^14 photons/s (1% bandwi dth multilayer monochromator) with an optimal 1x1 μm beam focus using ber yllium lenses/K-B mirrors. Beamline controls are from within MXCuBE\, with additional live feedback and CrystFEL autoprocessing pipelines to provide immediate feedback and rapid map generation. Sample pre-characterization is supported by an offline laser and spectroscopy lab in the secondary exp erimental hutch and dedicated sample environment and preparation labs.\nHe re we present the current status of MicroMAX beamline and recent developme nts in sample preparation and data handling under a variety of experimenta l contexts. This work emphasizes the technical developments for a highly f lexible TR-SSX end station in context of SSX/TR-SSX experiments already be ing conducted by the MicroMAX user community.\n\nMicroMAX is funded by the Novo Nordisk Foundation under the grant number NNF17CC0030666.\n\n[1] Gon zalez\, A.\, Krojer\, T.\, Nan\, J.\, Bjelcic\, M.\, Aggarwal\, S.\, Gorgi syan\, I.\, Milas\, M.\, Eguiraun\, M.\, Casadei\, C.\, Chenchiliyan\, M.\ , Jurgilaitis\, A.\, Kroon\, D.\, Ahn\, B.\, Ekstrom\, J. C.\, Aurelius\, O.\, Lang\, D.\, Ursby\, T. & Thunnissen\, M. M. G. M. (2025). J. Synchrot ron Rad. 32.\n[2] Shilova\, A.\, Lebrette\, H.\, Aurelius\, O.\, Nan\, J.\ , Welin\, M.\, Kovacic\, R.\, Ghosh\, S.\, Safari\, C.\, Friel\, R. J.\, M ilas\, M.\, Matej\, Z.\, Högbom\, M.\, Brändén\, G.\, Kloos\, M.\, Shoe man\, R. L.\, Doak\, B.\, Ursby\, T.\, Håkansson\, M.\, Logan\, D. T. & M ueller U. (2020). J. Synchrotron Rad.\, 27\, 1095.\n\nhttps://lindico453.s rv.lu.se/event/583/contributions/1851/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1851/ END:VEVENT BEGIN:VEVENT SUMMARY:Time-resolved X-ray crystallography on membrane proteins: Watching ions moving in time and space DTSTART;VALUE=DATE-TIME:20250923T070000Z DTEND;VALUE=DATE-TIME:20250923T073000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1845@lindico453.srv.lu.se DESCRIPTION:Speakers: Przemyslaw Nogly (Jagiellonian University in Krakow) \nP. Nogly\nDioscuri Centre for Structural Dynamics of Receptors\, Faculty of Biochemistry\, Biophysics and Biotechnology\, Jagiellonian University\ , Kraków\, Poland\; przemyslaw.nogly@uj.edu.pl \n\nChloride transport is an essential process maintaining ion balance across cell membranes\, cell growth\, and neuronal action potentials. However\, the molecular mechanism of the transport remains elusive. Among chloride transporters\, light-dri ven rhodopsins have gained attention as optogenetic tools to manipulate ne uronal signaling. We combined time-resolved serial crystallography at XFEL and synchrotron to provide a comprehensive view of chloride-pumping rhodo psin's structural dynamics and molecular mechanism throughout the transpor t cycle from 10 ps to 50 ms [1]. We traced transient anion binding sites\, obtained evidence for the mechanism of light energy utilization in transp ort\, and identified steric and electrostatic molecular gates ensuring uni directional transport. These structural insights provided the basis for mu tagenesis and functional study of the mechanistic features enabling finely controlled chloride transport across the cell membrane.\nFurthermore\, ou r recent study of a distinct photoreceptor\, Light-Oxygen-Voltage (LOV) do main\, will be introduced. The first insights into the structural dynamics of LOV photoactivation will be presented\, providing the basis for propos ing a molecular mechanism of a covalent thioether bond formation between a flavin mononucleotide cofactor and a reactive cysteine\, Cys57 (unpublish ed).\n\n[1] Mous\, S. et al. Science 375 (2022) 845\n\nhttps://lindico453. srv.lu.se/event/583/contributions/1845/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1845/ END:VEVENT BEGIN:VEVENT SUMMARY:Quantum refinement used for time-resolved crystallography DTSTART;VALUE=DATE-TIME:20250923T094500Z DTEND;VALUE=DATE-TIME:20250923T100000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1850@lindico453.srv.lu.se DESCRIPTION:Speakers: Gayathri Yuvaraj (Lund University)\nIn standard crys tallographic refinement of proteins\, the experimental data are normally n ot enough to unambiguously decide the positions of all atoms. Therefore\, the crystallographic data are supplemented by a set of empirical restraint s that ensure that bond lengths and angles make chemical sense. To obtain more accurate results\, we have suggested that this potential can be repla ced by more accurate quantum-mechanical (QM) calculations for a small\, bu t interesting part of the protein\, giving the method of quantum refinemen t.1 Our group has shown that quantum refinement can locally improve crysta l structures\,2 decide protonation state of metal-bound ligands\,3–6 oxi dation state of metal sites\,7\,8 detect photoreduction of metal ions7\,9 and solve scientific problems regarding what is really is seen in crystal structures.9–11 Several other groups have implemented this and similar a pproaches.12 We investigate how quantum refinement can be used for time-re solved crystallography. In time-resolved crystallography\, the obtained el ectron-density maps will typically involve a mixture of several states (un reacted state\, intermediates and products). Therefore\, the structures wi ll heavily depend on the empirical potential and the expectations of the c rystallographer. The QM calculations will give more accurate results\, esp ecially if there are intermediates with unusual (e.g. twisted) structures or if metal sites are involved (which are hard to describe with general re straints). Moreover\, we will couple the structural interpretations with e xpectations from kinetic models of the studied reaction. I will present so me preliminary applications on cytochrome c oxidase\, xylose isomerase and bacteriorhodopsin.\n\nReferences\n1. U. Ryde\, L. Olsen\, K. Nilsson\, 20 02\, J. Comput. Chem. 23\, 1058.\n2. U. Ryde\, K. Nilsson J. Am. Chem. Soc . 2003\, 125\, 14232.\n3. K. Nilsson\, U. Ryde\, J. Inorg. Biochem.\, 2004 \, 98\, 1539\n4. L. Cao\, O. Caldararu\, U. Ryde\, J. Phys. Chem B\, 2017\ , 121\, 8242.\n5. L. Cao\, O. Caldararu\, U. Ryde\, J. Chem. Theory Comput .\, 2018\, 14\, 6653.\n6. O. Caldararu\, M. Feldt\, D. Cioloboc\, M.-C.van Severen\, K. Starke\, E. Nordlander\, et al. Sci. Rep. 2018\, 8\, 4684\n7 . L. Rulíšek\, U. Ryde\, J. Phys. Chem. B\, 2006\, 110\, 11511\n8. L. Ca o\, Börner\, M. C.\, Bergmann\, J.\, Caldararu\, O. & U. Ryde\, Inorg. Ch em. 2019\, 58\, 9672.\n9. P. Söderhjelm\, U. Ryde\, J. Mol. Struct. Theoc hem\, 2006\, 770\, 199\n10. L. Cao\, O. Caldararu\, A. C. Rosenzweig\, U. Ryde\, 2018\, Angew. Chem. Int. Ed.\, 57\,162.\n11. J. Bergmann\, E. Oksan en & U. Ryde\, J. Biol. Inorg. Chem. 2021\, 26\, 341.\n12. J. Bergmann\, E . Oksanen\, U. Ryde\, Curr. Opin. Struct. Biol. 2022\, 72\, 18.\n\n\nAutho rs:\nGayathri Yuvaraj\, Ulf Ryde\nCo-authors:\nKristoffer Lundgren\, Esko Oksanen\n\nhttps://lindico453.srv.lu.se/event/583/contributions/1850/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1850/ END:VEVENT BEGIN:VEVENT SUMMARY:Modeling X-ray-Induced Heating at 4th-Generation MX Beamlines DTSTART;VALUE=DATE-TIME:20250923T091500Z DTEND;VALUE=DATE-TIME:20250923T094500Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1849@lindico453.srv.lu.se DESCRIPTION:Speakers: Michal Kepa (Paul Scherrer Institute)\nThe transitio n from 3rd to 4th generation synchrotrons—featuring diffraction-limited storage rings—has significantly expanded future possibilities for macrom olecular crystallography (MX). These upgrades\, characterized by reduced s ource divergence and increased electron bucket capacity\, have boosted bri lliance by up to two orders of magnitude. As a result\, next-generation MX beamlines\, such as ID29 (ESRF-EBS)\, BioCARS (APS-U)\, and MicroMAX (MAX IV)\, now deliver fluxes approaching 10^15 ph/s. These extremely high flu x (EHF) beamlines are increasingly optimized for time-resolved MX\, aiming for microsecond-scale resolution.\n\nOperating in previously unexplored d ose regimes (>50 GGy/s) raises new challenges. In my presentation\, I woul d like to share our study that focuses on beam-induced heating in microcry stals (<25 µm) exposed to EHF conditions. Thermal modeling indicates that such dose rates may cause significant temperature rises\, potentially imp acting data quality. Mitigation strategies include using top-hat beam prof iles and increasing both beam and crystal sizes to distribute dose more ev enly. The proposed model serves as a tool to support experimental design a nd optimize conditions for high-flux time-resolved MX. This of critical im portance for future multidimensional X-ray protein crystallography\, espec ially in enzymology\, where temperature is a key experimental variable. As such they will require precise temperature measurements\, as even a small change in temperature can affect the catalytic activity of an enzyme.\n\n \nAuthors: Michal Kepa\, John Beale\, Martin Appleby\n\nhttps://lindico453 .srv.lu.se/event/583/contributions/1849/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1849/ END:VEVENT BEGIN:VEVENT SUMMARY:GPCRs as Targets for Serial Crystallography DTSTART;VALUE=DATE-TIME:20250923T080000Z DTEND;VALUE=DATE-TIME:20250923T081500Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1847@lindico453.srv.lu.se DESCRIPTION:Speakers: Hannah Glover (leadXpro)\nUsing time-resolved serial crystallography to observe structural snapshots of protein dynamics at hi gh resolution is a method that is becoming gradually more commonplace. Adv ancements in method development for this technique have allowed a wider ra nge of proteins to be studied\; looking at processes spanning endogenous p hotoresponses\, enzyme kinetics and ligand binding. G protein-coupled rece ptors represent a pharmacologically relevant superfamily of proteins that are interesting targets for study with time-resolved serial crystallograph y. Data from time-resolved serial crystallography has the potential to enh ance the drug design process by revealing protein transitional states that can be either targeted or used to provide information about protein flexi bility. Our goal is to study the inherent dynamics of GPCRs critical for r eceptor function and to use this information to develop more targeted liga nds. Here\, we present the results of time-resolved serial crystallography experiments conducted at MaxIV and the SLS on the human A2a receptor. Thr ough synthetic photoswitches\, based on the marketed drug istradefylline f or the treatment of Parkinson’s disease\, light is used as a trigger to investigate the dynamics associated with ligand dissociation from the rece ptor orthosteric binding pocket. Our time-resolved data highlights key str uctural features involved in the transition upon ligand photoswitching. Th is includes the rearrangement of extracellular loops 2 and 3 that form a l id over the binding pocket\, which has been shown by molecular dynamic sim ulations\, crystal structures and kinetic analyses to be crucial for ligan d dissociation and long target resident time. Additionally\, lessons learn ed from this investigation\, in terms of experimental design and sample pr eparation\, can be applied to future projects using GPCRs as targets for s erial crystallography. Helping to lower the barrier of entry to time-resol ved serial crystallography and ultimately leading to more rationally desig ned drugs.\n\n\nCo-authors:\nTorben Saßmannshausen\, Quentin Bertrand\, M atilde Trabuco\, Chavdar Slavov\, Arianna Bacchin\, Fabio Andres\, Yasushi Kondo\, Robin Stipp\, Maximilian Wranik\, Georgii Khusainov\, Melissa Car rillo\, Demet Kekilli\, Jie Nan\, Ana Gonzalez\, Robert Cheng\, Werner Nei dhart\, Tobias Weinert\, Filip Leonarski\, Florian Dworkowski\, Michal Kep a\, Josef Wachtveitl\, Michael Hennig\, Joerg Standfuss\n\nhttps://lindico 453.srv.lu.se/event/583/contributions/1847/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1847/ END:VEVENT BEGIN:VEVENT SUMMARY:Using advanced crystallographic approaches to resolve how orange c arotenoid protein photocycle works DTSTART;VALUE=DATE-TIME:20250923T073000Z DTEND;VALUE=DATE-TIME:20250923T080000Z DTSTAMP;VALUE=DATE-TIME:20260525T143034Z UID:indico-contribution-215-1846@lindico453.srv.lu.se DESCRIPTION:Speakers: Volha Chukhutsina (Vrije Universiteit Amsterdam)\nht tps://lindico453.srv.lu.se/event/583/contributions/1846/ LOCATION:LINXS at The Loop URL:https://lindico453.srv.lu.se/event/583/contributions/1846/ END:VEVENT END:VCALENDAR