2R6S
Crystal structure of Gab protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-02-07 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 0.931 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 120.900, 120.900, 137.170 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.360 - 2.100 |
R-factor | 0.163 |
Rwork | 0.162 |
R-free | 0.19900 |
Starting model (for MR) | 1jr7 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.481 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.400 | 2.210 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.131 | 0.632 |
Number of reflections | 29931 | |
<I/σ(I)> | 10.5 | 2.4 |
Completeness [%] | 99.9 | 100 |
Redundancy | 4.9 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 298 | 1.6M ammonium sulphate, 0.1M bicine, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |