2PB7
Crystal Structure of the SRA domain of the human UHRF1 protein
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-01 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.8730, 0.9791, 0.9795, 0.9757 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 53.929, 53.929, 161.995 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.900 |
R-factor | 0.206 |
Rwork | 0.205 |
R-free | 0.22700 |
Structure solution method | MAD |
Starting model (for MR) | MAD model |
RMSD bond length | 0.010 |
RMSD bond angle | 1.375 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.080 | 0.350 |
Number of reflections | 22424 | |
<I/σ(I)> | 5 | |
Completeness [%] | 94.0 | 95.6 |
Redundancy | 5.6 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 295 | 14-19% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |