6U8G
BRD4-BD2 in complex with the cyclic peptide 3.1_2_AcK7toA
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 | 2018-08-23 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9537 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 58.712, 48.979, 114.152 |
Unit cell angles | 90.00, 101.66, 90.00 |
Refinement procedure
Resolution | 44.870 - 2.600 |
R-factor | 0.2444 |
Rwork | 0.242 |
R-free | 0.29650 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4lyi |
RMSD bond length | 0.001 |
RMSD bond angle | 0.462 |
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] | 47.390 | 2.720 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 19874 | 2433 |
<I/σ(I)> | 6.1 | |
Completeness [%] | 99.8 | |
Redundancy | 5.7 | |
CC(1/2) | 0.976 | 0.215 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 291 | 1.0 M Ammonium sulfate, 0.1 M BIS-Tris pH 5.5, 1 % w/v PEG 3350 |