Difference between revisions of "Serial Femtosecond Crystallography"

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(Created page with "TBD ==See Also== * XFEL * Chapman et al. [http://www.nature.com/nature/journal/v470/n7332/full/nature09750.html Femtosecond X-ray protein nanocrystallography] ''Nature'' ...")
 
 
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'''Serial Femtosecond Crystallography''' ('''SFX''') is the measurement of crystal structure by rapidly measuring incomplete diffraction patterns from a sequence of identical sample crystals. This is often performed at an [[XFEL]], where a sequence of crystals is dropped through the intense beam. With each snapshot, the crystal is measured shortly before it is destroyed by the intense beam ('diffract-and-destroy'). The sequence of diffraction patterns (slices through the three-dimensional [[reciprocal-space]]) can then be merged or analyzed collectively to determine the [[realspace]] crystal structure.
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As the brightness (high-flux and small spot-size) of modern [[synchrotron]]s increase, their measurements of crystals are also approaching the diffract-and-destroy regime; the same reconstruction methods are thus applicable to modern [[macromolecular crystallography]] [[beamlines]].
  
 
==See Also==
 
==See Also==
 
* [[XFEL]]
 
* [[XFEL]]
 
* Chapman et al. [http://www.nature.com/nature/journal/v470/n7332/full/nature09750.html Femtosecond X-ray protein nanocrystallography] ''Nature'' '''2011''', 470, 73-77. [http://dx.doi.org/10.1038/nature09750 doi: 10.1038/nature09750]
 
* Chapman et al. [http://www.nature.com/nature/journal/v470/n7332/full/nature09750.html Femtosecond X-ray protein nanocrystallography] ''Nature'' '''2011''', 470, 73-77. [http://dx.doi.org/10.1038/nature09750 doi: 10.1038/nature09750]
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*  Ilme Schlichting [http://journals.iucr.org/m/issues/2015/02/00/it5004/index.html Serial femtosecond crystallography: the first five years] ''IUCrJ'' '''2015''', 2 (2). [http://dx.doi.org/10.1107/S205225251402702X doi: 10.1107/S205225251402702X]
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*  Tao Zhang, Shifeng Jin, Yuanxin Gu, Yao He, Ming Li, Yang Li and Haifu Fan [http://journals.iucr.org/m/issues/2015/03/00/cw5006/index.html SFX analysis of non-biological polycrystalline samples] ''IUCrJ'' '''2015''', 2(3), 322-326. [http://dx.doi.org/10.1107/S2052252515002146 doi: 10.1107/S2052252515002146]
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*  Jörg Standfuss and John Spence [http://journals.iucr.org/m/issues/2017/02/00/me0641/index.html Serial crystallography at synchrotrons and X-ray lasers] ''IUCrJ'' '''2017''', 4 (2), 100-101. [http://dx.doi.org/https://doi.org/10.1107/S2052252517001877 doi: https://doi.org/10.1107/S2052252517001877]

Latest revision as of 10:48, 10 March 2017

Serial Femtosecond Crystallography (SFX) is the measurement of crystal structure by rapidly measuring incomplete diffraction patterns from a sequence of identical sample crystals. This is often performed at an XFEL, where a sequence of crystals is dropped through the intense beam. With each snapshot, the crystal is measured shortly before it is destroyed by the intense beam ('diffract-and-destroy'). The sequence of diffraction patterns (slices through the three-dimensional reciprocal-space) can then be merged or analyzed collectively to determine the realspace crystal structure.

As the brightness (high-flux and small spot-size) of modern synchrotrons increase, their measurements of crystals are also approaching the diffract-and-destroy regime; the same reconstruction methods are thus applicable to modern macromolecular crystallography beamlines.

See Also