Nanocrystallography measurements of early stage synthetic malaria pigment
- Univ. of Melbourne (Australia). ARC Centre of Excellenece in Advanced Molecular Imaging
- Commonwealth Scientific and Industrial Research Organization (CSIRO), Parkville VIC (Australia)
- La Trobe Univ., Melbourne, VIC (Australia). ARC Centre of Excellence in Advanced Molecular Imaging, La Trobe Inst. of Medical Research; Walter and Eliza Hall Inst. of Medical Research, Parkville, VIC (Australia); Commonwealth Scientific and Industrial Research Organization (CSIRO) Manufacturing Flagship, Parkville VIC (Australia)
- Univ. of Melbourne (Australia). Dept. of Biochemistry and Molecular Biology, Molecular Science and Biotechnology Inst.
- SLAC National Accelerator Lab., Menlo Park, CA (United States). Linac Coherent Light Source
- BioXFEL STC Buffalo, NY (United States)
- Brookhaven National Lab. (BNL), Upton, NY (United States)
- Commonwealth Scientific and Industrial Research Organization (CSIRO), Parkville VIC (Australia); La Trobe Univ., Melbourne, VIC (Australia). ARC Centre of Excellence in Advanced Molecular Imaging, La Trobe Inst. of Medical Research
- La Trobe Univ., Melbourne, VIC (Australia). ARC Centre of Excellence in Advanced Molecular Imaging, La Trobe Inst. of Medical Research
The recent availability of extremely intense, femtosecond X-ray free-electron laser (XFEL) sources has spurred the development of serial femtosecond nanocrystallography (SFX). Here, SFX is used to analyze nanoscale crystals of β-hematin, the synthetic form of hemozoin which is a waste by-product of the malaria parasite. This analysis reveals significant differences in β-hematin data collected during SFX and synchrotron crystallography experiments. To interpret these differences two possibilities are considered: structural differences between the nanocrystal and larger crystalline forms of β-hematin, and radiation damage. Simulation studies show that structural inhomogeneity appears at present to provide a better fit to the experimental data. If confirmed, these observations will have implications for designing compounds that inhibit hemozoin formation and suggest that, for some systems at least, additional information may be gained by comparing structures obtained from nanocrystals and macroscopic crystals of the same molecule.
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States); Brookhaven National Laboratory (BNL), Upton, NY (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC02-76SF00515; SC0012704
- OSTI ID:
- 1407496
- Alternate ID(s):
- OSTI ID: 1418317; OSTI ID: 1433955
- Report Number(s):
- BNL-203476-2018-JAAM; JACGAR; PII: S1600576717012663; TRN: US1703051
- Journal Information:
- Journal of Applied Crystallography (Online), Vol. 50, Issue 5; ISSN 1600-5767
- Publisher:
- International Union of CrystallographyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
TES X-ray Spectrometer at SLAC LCLS-II
|
journal | September 2018 |
Electrical and magnetic properties of hemozoin nanocrystals
|
journal | November 2018 |
An outlook on using serial femtosecond crystallography in drug discovery
|
journal | May 2019 |
Protein phase separation and determinants of in cell crystallization
|
journal | November 2019 |
Protein phase separation and determinants of in cell crystallization
|
text | January 2019 |
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