Add to ORKGMicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology
The bedrock of drug discovery and a key tool for understanding cellular function and drug mechanisms...
An exploration of the crystallographic theory of the relatively novel method of Microcrystal Electro...
In recent years, the success of serial femtosecond crystallography and the paucity of beamtime at X-...
MicroED uses very small three-dimensional protein crystals and electron diffraction for structure de...
These authors contributed equally to this work. MicroED uses very small three-dimensional protein cr...
We demonstrate that it is feasible to determine high-resolution protein structures by electron cryst...
Electron diffraction of extremely small three-dimensional crystals (MicroED) allows for structure de...
MicroED, a method at the intersection of X-ray crystallography and electron cryo-microscopy, has rap...
MicroED has recently emerged as a powerful method for the analysis of biological structures at atomi...
Structures of two globular proteins were determined ab initio using microcrystal electron diffractio...
MicroED is a method which combines cryo-EM sample preparation and instrumentation, with electron and...
Microcrystal electron diffraction (MicroED) was first coined and developed in 2013 at the Janelia Re...
Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from su...
Thesis (Ph.D.)--University of Washington, 2014Crystallographic methods for protein structure determi...
It is now possible to routinely determine atomic resolution structures by electron cryo-microscopy (...
The bedrock of drug discovery and a key tool for understanding cellular function and drug mechanisms...
An exploration of the crystallographic theory of the relatively novel method of Microcrystal Electro...
In recent years, the success of serial femtosecond crystallography and the paucity of beamtime at X-...
MicroED uses very small three-dimensional protein crystals and electron diffraction for structure de...
These authors contributed equally to this work. MicroED uses very small three-dimensional protein cr...
We demonstrate that it is feasible to determine high-resolution protein structures by electron cryst...
Electron diffraction of extremely small three-dimensional crystals (MicroED) allows for structure de...
MicroED, a method at the intersection of X-ray crystallography and electron cryo-microscopy, has rap...
MicroED has recently emerged as a powerful method for the analysis of biological structures at atomi...
Structures of two globular proteins were determined ab initio using microcrystal electron diffractio...
MicroED is a method which combines cryo-EM sample preparation and instrumentation, with electron and...
Microcrystal electron diffraction (MicroED) was first coined and developed in 2013 at the Janelia Re...
Serial X-ray crystallography at free-electron lasers allows to solve biomolecular structures from su...
Thesis (Ph.D.)--University of Washington, 2014Crystallographic methods for protein structure determi...
It is now possible to routinely determine atomic resolution structures by electron cryo-microscopy (...
The bedrock of drug discovery and a key tool for understanding cellular function and drug mechanisms...
An exploration of the crystallographic theory of the relatively novel method of Microcrystal Electro...
In recent years, the success of serial femtosecond crystallography and the paucity of beamtime at X-...