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SUMMARY:From Static to Dynamic: Evolving Methods in Protein Structure Dete
 rmination
DTSTART;VALUE=DATE-TIME:20250922T124000Z
DTEND;VALUE=DATE-TIME:20250922T131000Z
DTSTAMP;VALUE=DATE-TIME:20260526T034239Z
UID:indico-contribution-1828@lindico453.srv.lu.se
DESCRIPTION:Speakers: Aina Cohen (Stanford Synchrotron Radiation Lightsour
 ce)\n(representing the entire SSRL-SMB team)\nStructural Molecular Biology
  (SMB)\, Stanford Synchrotron Radiation Lightsource (SSRL)\, SLAC National
  Accelerator Laboratory\, Stanford University\, Menlo Park\, United States
  of America\n\nStructural biologists are undertaking increasingly challeng
 ing projects including the study of membrane proteins and complex multi-co
 mponent machines. Structural investigations are also transitioning beyond 
 solving a single static structure\, to the application of a series of sequ
 ential structural snapshots to provide details of the atomic positions and
  motions that define the relationships involved in molecular recognition\,
  transition state stabilization\, and other aspects of the biocatalytic pr
 ocess. The success of these experiments requires careful optimization of s
 amples and experimental setups\, often involving multiple experiments at t
 he laboratory bench and the beamline\, where automation serves as an enabl
 ing technology to efficiently deliver multiple crystals and meet stringent
  timing requirements. \nDevelopments at SSRL and LCLS-MFX will be presente
 d that tackle challenges involved in the study of metalloenzymes\, the use
  of small and radiation-sensitive crystals\, and to perform time-resolved 
 crystallography. To facilitate the handling and optimization of delicate c
 rystals\, new in situ crystallization and remote data collection schemes h
 ave been released that avoid direct manipulation of crystals\, support rob
 otic sample exchange\, and allow full rotational access of the sample in a
  controlled humidity environment. By simplifying crystal handling and tran
 sport at near-physiological temperatures\, these technologies remove barri
 ers to enable more widespread use of serial crystallography methods for st
 udies of metalloenzyme structure and protein dynamics. Strategies for time
 -resolved measurements and data analysis tools that provide rapid feedback
  for experimental optimization during fast-paced experiments will also be 
 described.\n\nhttps://lindico453.srv.lu.se/event/583/contributions/1828/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1828/
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