4MT8
Structure of the ERS1 dimerization and histidine phosphotransfer domain from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-03-05 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.923 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.042, 98.747, 77.177 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.300 - 1.900 |
R-factor | 0.1964 |
Rwork | 0.195 |
R-free | 0.22650 |
Structure solution method | SAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.509 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | PHENIX ((phenix.refine: dev_1092)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.300 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Number of reflections | 22944 | |
<I/σ(I)> | 14.3 | |
Completeness [%] | 99.4 | 97.6 |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.18 M l-proline, 0.1 M HEPES pH 7.5, 9% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 293K |