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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-0E35-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-0E39-2
Genre: Journal Article

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 Creators:
Barends, T. R., Author
Foucar, L., Author
Shoeman, R. L., Author
Bari, S.1, Author              
Epp, S. W., Author
Hartmann, R., Author
Hauser, G., Author
Huth, M., Author
Kieser, C., Author
Lomb, L., Author
Motomura, K., Author
Nagaya, K., Author
Schmidt, C., Author
Strecker, R., Author
Anielski, D., Author
Boll, R.1, Author              
Erk, B., Author
Fukuzawa, H., Author
Hartmann, E., Author
Hatsui, T., Author
Holl, P., AuthorInubushi, Y., AuthorIshikawa, T., AuthorKassemeyer, S., AuthorKaiser, C., AuthorKoeck, F., AuthorKunishima, N., AuthorKurka, M., AuthorRolles, D.1, Author              Rudek, B., AuthorRudenko, A., AuthorSato, T., AuthorSchroeter, C. D., AuthorSoltau, H., AuthorStrueder, L., AuthorTanaka, T., AuthorTogashi, T., AuthorTono, K., AuthorUllrich, J., AuthorYase, S., AuthorWada, S. I., AuthorYao, M., AuthorYabashi, M., AuthorUeda, K., AuthorSchlichting, I., Author more..
Affiliations:
1Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society, ou_578564              

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Free keywords: anomalous diffraction; free-electron lasers; protein crystallography
 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.

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Language(s): eng - English
 Dates: 2013-04-112013-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1107/S0907444913002448
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Title: Acta Crystallographica D
Source Genre: Journal
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Pages: - Volume / Issue: 69 (5) Sequence Number: - Start / End Page: 838 - 842 Identifier: -