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Title: Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging

For laboratory and synchrotron based X-ray sources, radiation damage has posed a significant barrier to obtaining high-resolution structural data from biological macromolecules. The problem is particularly acute for micron-sized crystals where the weaker signal often necessitates the use of higher intensity beams to obtain the relevant data. Here, we employ a combination of techniques, including Bragg coherent diffractive imaging to characterise the radiation induced damage in a micron-sized protein crystal over time. The approach we adopt here could help screen for potential protein crystal candidates for measurement at X-ray free election laser sources.
 [1] ;  [2] ;  [1] ;  [3] ;  [4] ;  [5] ;  [5] ;  [6]
  1. La Trobe Univ., Melbourne (Australia); CSIRO Manufacturing Flagship, Parkville (Australia)
  2. La Trobe Univ., Melbourne (Australia)
  3. Univ. of Oxford, Oxford (United Kingdom)
  4. SLAC National Accelerator Lab., Menlo Park, CA (United States); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
  5. Argonne National Lab. (ANL), Argonne, IL (United States)
  6. La Trobe Univ., Melbourne (Australia); Melbourne Centre for Nanofabrication, Melbourne (Australia)
Publication Date:
OSTI Identifier:
Grant/Contract Number:
Accepted Manuscript
Journal Name:
Structural Dynamics
Additional Journal Information:
Journal Volume: 2; Journal Issue: 4; Journal ID: ISSN 2329-7778
American Crystallographic Association/AIP
Research Org:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY proteins; radiation damage; x-ray diffraction; crystal structure; reciprocal space