2WP2
Structure of Brdt bromodomain BD1 bound to a diacetylated histone H4 peptide.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 49.293, 61.224, 97.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 44.000 - 2.370 |
| R-factor | 0.217 |
| Rwork | 0.217 |
| R-free | 0.26100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | BROMODOMAIN BD2 FROM BRDT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.154 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.000 | 2.400 |
| High resolution limit [Å] | 2.370 | 2.370 |
| Rmerge | 0.140 | 0.410 |
| Number of reflections | 12142 | |
| <I/σ(I)> | 7.1 | 2.3 |
| Completeness [%] | 96.7 | 63.3 |
| Redundancy | 3.3 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 15 MG/ML BRDT-BD1 PROTEIN WAS MIXED WITH H4-ACK5/K8 PEPTIDE IN A 1:20 MOLAR RATIO. CRYSTALLIZATION WAS BY THE HANGING DROP VAPOUR DIFFUSION METHOD FROM 2.4 M AMMONIUM SULFATE, 0.1 M HEPES PH 7. |
