7LHY
Caenorhabditis elegans SWSN-4 (SMARCA4-BRG1) ATPase Bromodomain in complex with a modified histone H3, N6-epsilon-acetyl-L-lysine 14 (H3K14ac) polypeptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 170 |
Detector technology | PIXEL |
Collection date | 2016-10-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 69.064, 69.064, 55.320 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 48.840 - 1.300 |
R-factor | 0.1822 |
Rwork | 0.181 |
R-free | 0.19780 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2grc |
RMSD bond length | 0.027 |
RMSD bond angle | 2.341 |
Data reduction software | HKL-2000 (2.3.8) |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.340 |
High resolution limit [Å] | 1.290 | 1.290 |
Rmerge | 0.075 | 0.930 |
Rmeas | 0.078 | 0.970 |
Rpim | 0.023 | 0.300 |
Number of reflections | 34008 | 3306 |
<I/σ(I)> | 13.9 | |
Completeness [%] | 99.7 | 100 |
Redundancy | 13.8 | 12 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 277 | 35% total PEG concentration, divided equally among PEG 400, PEG 550 MME, PEG 600 and PEG 1,000. There was no buffer in this condition, but the protein was purified in 10 mM HEPES, pH 7.3 |