Low-dose X-ray structure analysis of cytochrome c oxidase utilizing high-energy X-rays.
J Synchrotron Radiat
; 26(Pt 4): 912-921, 2019 Jul 01.
Article
in En
| MEDLINE
| ID: mdl-31274413
ABSTRACT
To investigate the effect of high-energy X-rays on site-specific radiation-damage, low-dose diffraction data were collected from radiation-sensitive crystals of the metal enzyme cytochrome c oxidase. Data were collected at the Structural Biology I beamline (BL41XU) at SPring-8, using 30â
keV X-rays and a highly sensitive pixel array detector equipped with a cadmium telluride sensor. The experimental setup of continuous sample translation using multiple crystals allowed the average diffraction weighted dose per data set to be reduced to 58â
kGy, and the resulting data revealed a ligand structure featuring an identical bond length to that in the damage-free structure determined using an X-ray free-electron laser. However, precise analysis of the residual density around the ligand structure refined with the synchrotron data showed the possibility of a small level of specific damage, which might have resulted from the accumulated dose of 58â
kGy per data set. Further investigation of the photon-energy dependence of specific damage, as assessed by variations in UV-vis absorption spectra, was conducted using an on-line spectrometer at various energies ranging from 10 to 30â
keV. No evidence was found for specific radiation damage being energy dependent.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
X-Rays
/
Crystallography, X-Ray
/
Electron Transport Complex IV
Language:
En
Journal:
J Synchrotron Radiat
Journal subject:
RADIOLOGIA
Year:
2019
Document type:
Article
Affiliation country:
Japan