3UIM
Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-07-10 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 70.110, 74.700, 71.924 |
Unit cell angles | 90.00, 93.72, 90.00 |
Refinement procedure
Resolution | 37.350 - 2.200 |
R-factor | 0.2366 |
Rwork | 0.234 |
R-free | 0.27700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2nry |
RMSD bond length | 0.008 |
RMSD bond angle | 1.384 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 19638 |
Completeness [%] | 99.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | PEG3350, sodium citrate, ammonium sulfate, HEPES , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |