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SUMMARY:Standard Sample Preparation and Characterization for Serial Crysta
 llography
DTSTART;VALUE=DATE-TIME:20250922T171000Z
DTEND;VALUE=DATE-TIME:20250922T172000Z
DTSTAMP;VALUE=DATE-TIME:20260526T203227Z
UID:indico-contribution-1842@lindico453.srv.lu.se
DESCRIPTION:Speakers: Christina Schmidt (European XFEL)\nSerial crystallog
 raphy (SX) has been a revolutionary technique in structural biology for mo
 re than a decade\, providing insights into the structures and dynamics of 
 biomolecules at room temperature. Using intense ultra-short X-ray pulses\,
  SX made the collection of diffraction data from micron-sized crystals pos
 sible\, avoiding radiation damage and allowing for the capture of transien
 t states and intermediates in biological reactions. The success of SX expe
 riments heavily relies on the quality of the sample.\nStandard samples in 
 SX research provide critical roles. First\, the commissioning of new beaml
 ine devices needs well-characterized samples. By providing consistent and 
 reproducible diffraction patterns\, the standard samples help in the calib
 ration of new devices and verification of their performance. Secondly\, th
 ey are required for the validation of experimental setups\, ensuring that 
 all components\, from sample delivery systems to data acquisition software
 \, function correctly.\nIn this study\, we present detailed protocols for 
 the preparation of lysozyme\, myoglobin\, iq-mEmerald\, and photoactive ye
 llow protein (PYP) crystals. These proteins were selected as standard samp
 les due to their robust crystallization properties and suitability for a w
 ide range of SX experiments. Through the optimization of existing protocol
 s\, we achieved high-quality crystal samples with improved yield\, specifi
 cally for SX applications.\n\n\nAuthors: Christina Schmidt\, Huijong Han\n
 \nhttps://lindico453.srv.lu.se/event/583/contributions/1842/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1842/
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