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SUMMARY:Protein structure determination using X-ray lasers - Professor Hen
 ry Chapman\, University of Hamburg\, Germany
DTSTART:20130306T150000Z
DTEND:20130306T160000Z
UID:TALK43318@talks.cam.ac.uk
CONTACT:Penny Peck
DESCRIPTION:X-ray free-electron lasers (FELs) are very large machines that
  produce the briefest and most intense flashes of X-rays.  The X-ray beam 
 at the world’s first hard X-ray FEL\, the Linac Coherent Light Source in
  Stanford\, is so intense that it melts a hole through 3 mm of stainless s
 teel in under a second.   Yet we apply this beam to elucidate the molecula
 r structure of proteins and obtain images of virus particles\, which are c
 ertainly more delicate than steel.  In fact\, these objects are completely
  vaporised in the beam\, and we overcome the problem of this radiation dam
 age by using the short X-ray pulses to outrun the explosion.  We have show
 n that we obtain atomic-resolution information with pulses of 30 fs or sho
 rter.  This “diffraction before destruction” technique allows us to de
 termine the molecular structures of proteins that cannot be grown into lar
 ge enough crystals or are too radiation sensitive for conventional X-ray c
 rystallography with synchrotron radiation.  We aim to push this technique 
 to smaller and smaller samples--all the way down to the single molecule.
LOCATION:Sackler Lecture Theatre (Level 7) Wellcome Trust/MRC Building\, A
 ddenbrooke's Site
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