6ULS
BRD4-BD1 in complex with the a diacetylated-E2F1 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-06-30 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.953700 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 48.309, 50.350, 54.246 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.900 - 1.500 |
R-factor | 0.172 |
Rwork | 0.170 |
R-free | 0.20430 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4lyi |
RMSD bond length | 0.008 |
RMSD bond angle | 0.977 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.14_3260) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.310 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Number of reflections | 21857 | 1070 |
<I/σ(I)> | 32.5 | |
Completeness [%] | 100.0 | |
Redundancy | 12.8 | |
CC(1/2) | 0.999 | 0.982 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 291 | 0.1 M MMT pH 7.0, 25% w/v PEG 1500 |