Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.9
Classification:HYDROLASE
Release Date:2012-06-13
Deposition Date:2012-04-24
Revision Date:2012-08-08#2015-11-18#2017-11-15#2018-02-14
Molecular Weight:14389.6
Macromolecule Type:Protein
Residue Count:129
Atom Site Count:1003
DOI:10.2210/pdb4et8/pdb
Abstract:
Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
Resolution:1.9
Classification:HYDROLASE
Release Date:2012-06-13
Deposition Date:2012-04-24
Revision Date:2012-08-08#2015-11-18#2017-11-15#2018-02-14
Molecular Weight:14389.6
Macromolecule Type:Protein
Residue Count:129
Atom Site Count:1003
DOI:10.2210/pdb4et8/pdb
Abstract:
Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
| Date made available | 2012 |
|---|---|
| Publisher | RCSB-PDB |