Macromolecular crystallography at synchrotron radiation sources: current status and future developments
EMH Duke, LN Johnson - Proceedings of the Royal …, 2010 - royalsocietypublishing.org
X-ray diffraction with synchrotron radiation (SR) has revealed the atomic structures of
numerous biological macromolecules including proteins and protein complexes, nucleic …
numerous biological macromolecules including proteins and protein complexes, nucleic …
Global radiation damage: temperature dependence, time dependence and how to outrun it
M Warkentin, JB Hopkins, R Badeau… - Journal of …, 2013 - journals.iucr.org
A series of studies that provide a consistent and illuminating picture of global radiation
damage to protein crystals, especially at temperatures above∼ 200 K, are described. The …
damage to protein crystals, especially at temperatures above∼ 200 K, are described. The …
Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites
Understanding the structure and dynamics of membrane proteins in their native,
hydrophobic environment is important to understanding how these proteins function. EPR …
hydrophobic environment is important to understanding how these proteins function. EPR …
[PDF][PDF] Lifetimes and spatio-temporal response of protein crystals in intense X-ray microbeams
Serial synchrotron-based crystallography using intense microfocused X-ray beams, fast-
framing detectors and protein microcrystals held at 300 K promises to expand the range of …
framing detectors and protein microcrystals held at 300 K promises to expand the range of …
[PDF][PDF] Determining biomolecular structures near room temperature using X-ray crystallography: concepts, methods and future optimization
RE Thorne - Acta Crystallographica Section D: Structural Biology, 2023 - journals.iucr.org
For roughly two decades, cryocrystallography has been the overwhelmingly dominant
method for determining high-resolution biomolecular structures. Competition from single …
method for determining high-resolution biomolecular structures. Competition from single …
Radiation decay of thaumatin crystals at three X-ray energies
D Liebschner, G Rosenbaum, M Dauter… - … Section D: Biological …, 2015 - journals.iucr.org
Radiation damage is an unavoidable obstacle in X-ray crystallographic data collection for
macromolecular structure determination, so it is important to know how much radiation a …
macromolecular structure determination, so it is important to know how much radiation a …
[PDF][PDF] Ice formation and solvent nanoconfinement in protein crystals
Ice formation within protein crystals is a major obstacle to the cryocrystallographic study of
protein structure, and has limited studies of how the structural ensemble of a protein evolves …
protein structure, and has limited studies of how the structural ensemble of a protein evolves …
Solvent flows, conformation changes and lattice reordering in a cold protein crystal
When protein crystals are abruptly cooled, the unit-cell, protein and solvent-cavity volumes
all contract, but the volume of bulk-like internal solvent may expand. Outflow of this solvent …
all contract, but the volume of bulk-like internal solvent may expand. Outflow of this solvent …