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Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser.

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Bari,  S.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

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Boll,  R.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

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Rolles,  D.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

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2367369_Suppl.hkl
(Supplementary material), 149KB

Citation

Barends, T. R., Foucar, L., Shoeman, R. L., Bari, S., Epp, S. W., Hartmann, R., et al. (2013). Anomalous signal from S atoms in protein crystallographic data from an X-ray free-electron laser. Acta Crystallographica D, 69(5), 838-842. doi:10.1107/S0907444913002448.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-0E35-A
Abstract
X-ray free-electron lasers (FELs) enable crystallographic data collection using extremely bright femtosecond pulses from microscopic crystals beyond the limitations of conventional radiation damage. This diffraction-before-destruction approach requires a new crystal for each FEL shot and, since the crystals cannot be rotated during the X-ray pulse, data collection requires averaging over many different crystals and a Monte Carlo integration of the diffraction intensities, making the accurate determination of structure factors challenging. To investigate whether sufficient accuracy can be attained for the measurement of anomalous signal, a large data set was collected from lysozyme microcrystals at the newly established `multi-purpose spectroscopy/imaging instrument' of the SPring-8 Ångstrom Compact Free-Electron Laser (SACLA) at RIKEN Harima. Anomalous difference density maps calculated from these data demonstrate that serial femtosecond crystallography using a free-electron laser is sufficiently accurate to measure even the very weak anomalous signal of naturally occurring S atoms in a protein at a photon energy of 7.3 keV.