$cryogenic temp xray diffraction$

#Cryogenic temp xray diffraction serial#

Temperature can induce pH changes 10 and the addition of cryo-protectants can lead to structural artifacts in cryogenic structures 11. However, they result in altered structural conformations of the side chains and loop regions that can potentially deviate significantly from those obtained at near physiological temperature 9. The increased unit-cell volume results in non-isomorphism, leading to difficulties in structure determination 8.Ĭryogenic temperature diffraction data collection allows improved resolution by protecting crystals from radiation damage caused by powerful X-ray sources. In addition, global radiation damage can perturb diffraction patterns and increase the unit-cell volume and mosaicity. To overcome this, data collection can be performed at cryogenic temperatures however, cryogenic data collection does not eliminate radiation damage completely but can itself perturb crystal lattice and protein structures 7. This damage results in the reduction of diffraction data quality and can lead to compositional and conformational structural perturbations 6. The X-ray photons cause Auger decay and K-shell photoionization and may generate reactive oxygen species that can propagate throughout the crystal 4, 5. However, this approach can result in radiation damage within proteins due to primary X-ray absorption during diffraction data collection 4, 5. Conventional single crystal X-ray crystallography has led to many scientific developments and discoveries in basic science and medicine and is still considered a relevant structural biology technique to many biologists 2, 3. X-ray crystallography has played a dominant role in understanding the structural dynamics of biomacromolecules and elucidating molecular mechanisms of many important biological processes in the past five decades 1. Turkish DeLight provides robust and rapid ambient temperature biomacromolecular structure determination with limited radiation damage. Combined with our previous cryogenic structure (PDB ID: 7Y6A), the ambient temperature structure provides invaluable information about the structural dynamics of the lysozyme. The complete dataset was collected in 18.5 min with resolution extending to 2.39 Å and 100% completeness. We also present the first ambient temperature lysozyme structure determined at the Turkish light source ( Turkish DeLight). 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.

#Cryogenic temp xray diffraction serial#

Obtaining a high volume of well-diffracting, sufficient-size crystals while mitigating radiation damage remains a critical bottleneck of serial crystallography. 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. High-resolution biomacromolecular structure determination is essential to better understand protein function and dynamics. Scientific Reports volume 13, Article number: 8123 ( 2023) Rapid and efficient ambient temperature X-ray crystal structure determination at Turkish Light Source

$cryogenic temp xray diffraction$