Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography

Coughlan, H. D.; Darmanin, C.; Kirkwood, H. J.; Phillips, N. W.; Hoxley, D.; Clark, J. N.; Vine, D. J.; Hofmann, F.; Harder, R. J.; Maxey, E.; Abbey, B.

doi:10.1107/s1600577516017525

Title: Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography

Journal Article · Sun Jan 01 00:00:00 EST 2017 · Journal of Synchrotron Radiation (Online)

DOI:https://doi.org/10.1107/s1600577516017525· OSTI ID:1348845

Coughlan, H. D. ^[1]; Darmanin, C. ^[2]; Kirkwood, H. J. ^[2]; Phillips, N. W. ^[1];

^[2]; Clark, J. N. ^[3]; Vine, D. J. ^[4]; Hofmann, F. ^[5]; Harder, R. J. ^[6];

^[6]; Abbey, B. ^[2]

La Trobe Univ., Victoria (Australia); CSIRO Manufacturing Flagship, Parkville (Australia)
La Trobe Univ., Victoria (Australia)
SLAC National Accelerator Lab., Menlo Park, CA (United States); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Univ. of Oxford, Oxford (United Kingdom)
Argonne National Lab. (ANL), Argonne, IL (United States)

The proliferation of extremely intense synchrotron sources has enabled ever higher-resolution structures to be obtained using data collected from smaller and often more imperfect biological crystals. Synchrotron beamlines now exist that are capable of measuring data from single crystals that are just a few micrometres in size. This provides renewed motivation to study and understand the radiation damage behaviour of small protein crystals. Reciprocal-space mapping and Bragg coherent diffractive imaging experiments have been performed on cryo-cooled microcrystals of hen egg-white lysozyme as they undergo radiation damage. Several well established metrics, such as intensity-loss and lattice expansion, are applied to the diffraction data and the results are compared with several new metrics that can be extracted from the coherent imaging experiments. Individually some of these metrics are inconclusive. However, combining metrics, the results suggest that radiation damage behaviour in protein micro-crystals differs from that of larger protein crystals and may allow them to continue to diffract for longer. As a result, a possible mechanism to account for these observations is proposed.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1348845

Journal Information:: Journal of Synchrotron Radiation (Online), Vol. 24, Issue 1; ISSN 1600-5775

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

Citation Metrics:

Cited by: 13 works

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