3BOR
Crystal structure of the DEADc domain of human translation initiation factor 4A-2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-12-06 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97242 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 58.093, 80.102, 42.740 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.850 |
R-factor | 0.187 |
Rwork | 0.185 |
R-free | 0.22600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2g9n |
RMSD bond length | 0.015 |
RMSD bond angle | 1.344 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (refmac_5.3.0037) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.000 | 40.000 | 1.920 |
High resolution limit [Å] | 1.850 | 3.980 | 1.850 |
Rmerge | 0.133 | 0.068 | 0.656 |
Number of reflections | 17895 | ||
<I/σ(I)> | 6.6 | ||
Completeness [%] | 100.0 | 99.8 | 99.9 |
Redundancy | 11.4 | 10.9 | 10.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.3 | 291 | 25% PEG 3350, 0.1M Bis-Tris, 0.2M Ammonium acetate. Chymotrypsin was added to the crystallization sample at a molar ratio of approx. 1:100, pH 7.3, VAPOR DIFFUSION, temperature 291K |