4MTX
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 ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-11-12 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9919 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 65.911, 69.193, 108.256 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.700 - 2.150 |
R-factor | 0.2009 |
Rwork | 0.198 |
R-free | 0.25060 |
Structure solution method | UV-RIP |
RMSD bond length | 0.009 |
RMSD bond angle | 1.208 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHELX |
Refinement software | PHENIX ((phenix.refine: dev_1092)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.700 | 2.227 |
High resolution limit [Å] | 2.150 | 2.150 |
Number of reflections | 27137 | |
Completeness [%] | 98.1 | 99.7 |
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, 0.12 M sodium citrate, VAPOR DIFFUSION, SITTING DROP, temperature 293K |