5GQ0
Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL18U1 |
Synchrotron site | SSRF |
Beamline | BL18U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-09-13 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.979 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 100.127, 100.127, 164.814 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 37.004 - 2.310 |
R-factor | 0.1906 |
Rwork | 0.189 |
R-free | 0.23050 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5a10 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.177 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.370 |
High resolution limit [Å] | 2.308 | 2.310 |
Rmerge | 0.139 | |
Number of reflections | 37659 | |
<I/σ(I)> | 22.5 | |
Completeness [%] | 99.4 | |
Redundancy | 21.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 0.2M potassium sodium tartrate tetrahydrate pH 7.4, 20% PEG3350 |