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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:20260526T034238Z
UID:indico-contribution-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/
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