5ITA
Crystal Structure of BRAF Kinase Domain Bound to AZ-VEM
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 31-ID |
Synchrotron site | APS |
Beamline | 31-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-10-12 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9797 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 52.105, 103.817, 110.567 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.730 - 1.950 |
R-factor | 0.197 |
Rwork | 0.195 |
R-free | 0.24400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3og7 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.002 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2155)) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.949 |
Number of reflections | 44542 |
<I/σ(I)> | 26.9 |
Completeness [%] | 99.7 |
Redundancy | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291.1 | PEG3350 |