4Q96
CID of human RPRD1B in complex with an unmodified CTD peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-19 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 0.9179 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.653, 134.707, 55.706 |
Unit cell angles | 90.00, 106.64, 90.00 |
Refinement procedure
Resolution | 44.654 - 1.850 |
R-factor | 0.2389 |
Rwork | 0.238 |
R-free | 0.27090 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.076 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.20) |
Phasing software | MOLREP |
Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 67.353 | 44.654 | 1.950 |
High resolution limit [Å] | 1.848 | 5.850 | 1.850 |
Rmerge | 0.037 | 0.851 | |
Total number of observations | 7701 | 36772 | |
Number of reflections | 66812 | ||
<I/σ(I)> | 10.8 | 14.5 | 0.9 |
Completeness [%] | 99.9 | 99.5 | 100 |
Redundancy | 3.8 | 3.6 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 7.5 | 291 | 25% PEG-1500, 0.2M ammonium sulfate, 0.1M HEPES, pH 7.5, vapor diffusion, temperature 291K |