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Title: Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source

Journal Article · · Scientific Reports
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  1. Koc Univ., Istanbul (Turkey)
  2. Koc Univ., Istanbul (Turkey); Gebze Technical University (Turkey); University of Health Sciences, Istanbul (Turkey)
  3. Koc Univ., Istanbul (Turkey); Istanbul Technical University (Turkey)
  4. Koc Univ., Istanbul (Turkey); Istanbul Arel University (Turkey)
  5. Koc Univ., Istanbul (Turkey); Yıldız Technical University, Istanbul (Turkey)
  6. University of Health Sciences, Istanbul (Turkey)
  7. Kumamoto University (Japan); Science Farm Ltd. (Japan)
  8. Kumamoto University (Japan)
  9. University of Health Sciences, Istanbul (Turkey); Marmara Research Center (MAM) (Turkey)
  10. Koc Univ., Istanbul (Turkey); Kumamoto University (Japan); Science Farm Ltd. (Japan)
  11. Bahcesehir University, Istanbul (Turkey)
  12. Izmir Biomedicine and Genome Center (Turkey); Dokuz Eylul University (Turkey)
  13. Ege University (Turkey)
  14. Ankara University (Turkey); Univ. of Bristol (United Kingdom)
  15. Koc Univ., Istanbul (Turkey); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
+ Show Author Affiliations

High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Serial crystallography is an emerging structural biology technique which has fundamental limitations due to either sample volume requirements or immediate access to the competitive X-ray beamtime. Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography. As an alternative, we introduce the plate-reader module adapted for using a 72-well Terasaki plate for biomacromolecule structure determination at a convenience of a home X-ray source. We also present the first ambient temperature lysozyme structure determined at the Turkish light source (Turkish DeLight). The complete dataset was collected in 18.5 min with resolution extending to 2.39 Å and 100% completeness. Combined with our previous cryogenic structure (PDB ID: 7Y6A), the ambient temperature structure provides invaluable information about the structural dynamics of the lysozyme. Turkish DeLight provides robust and rapid ambient temperature biomacromolecular structure determination with limited radiation damage.

Research Organization:
SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
Sponsoring Organization:
USDOE Office of Science (SC); National Science Foundation (NSF)
Grant/Contract Number:
AC02-76SF00515
OSTI ID:
2001432
Journal Information:
Scientific Reports, Vol. 13, Issue 1; ISSN 2045-2322
Publisher:
Nature Publishing GroupCopyright Statement
Country of Publication:
United States
Language:
English

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59 BASIC BIOLOGICAL SCIENCES
proteins
x-ray crystallography