Description
Experimental Technique/Method:ELECTRON CRYSTALLOGRAPHY
Resolution:2.5
Classification:HYDROLASE
Release Date:2014-08-13
Deposition Date:2014-03-18
Revision Date:2014-08-20#2014-09-10#2015-04-08
Molecular Weight:14331.16
Macromolecule Type:Protein
Residue Count:129
Atom Site Count:1001
DOI:10.2210/pdb3j6k/pdb
Abstract:
MicroED 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.
Resolution:2.5
Classification:HYDROLASE
Release Date:2014-08-13
Deposition Date:2014-03-18
Revision Date:2014-08-20#2014-09-10#2015-04-08
Molecular Weight:14331.16
Macromolecule Type:Protein
Residue Count:129
Atom Site Count:1001
DOI:10.2210/pdb3j6k/pdb
Abstract:
MicroED 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.
| Date made available | Aug 13 2014 |
|---|---|
| Publisher | RCSB-PDB |