2HQE
Crystal structure of human P100 Tudor domain: Large fragment
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-06-16 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9790 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.931, 93.413, 95.279 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.240 - 2.000 |
R-factor | 0.23427 |
Rwork | 0.233 |
R-free | 0.24919 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2hqx |
RMSD bond length | 0.009 |
RMSD bond angle | 1.080 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 44.000 | 1.860 |
High resolution limit [Å] | 1.800 | 1.800 |
Number of reflections | 29102 | |
<I/σ(I)> | 12.7 | 12.1 |
Completeness [%] | 89.1 | 100 |
Redundancy | 8.4 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.2 | 291 | 2 micor liter drops containing equal volumes of protein solution (10.0 mg/ml) and precipitate solution (20% PEG 8000, 100.0 MM Phosphate, 0.1M Hepes), pH 4.2, VAPOR DIFFUSION, SITTING DROP, temperature 291K |