5LKX
Crystal structure of the p300 acetyltransferase catalytic core with propionyl-coenzyme A.
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 | PIXEL |
| Collection date | 2015-11-28 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.872600 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 93.810, 155.260, 109.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.520 |
| R-factor | 0.20828 |
| Rwork | 0.207 |
| R-free | 0.23944 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bhw |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.321 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.520 | 2.520 |
| Rmeas | 0.150 | 1.105 |
| Number of reflections | 27348 | |
| <I/σ(I)> | 10.49 | 1.48 |
| Completeness [%] | 99.5 | 98.3 |
| Redundancy | 5.2 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | Tris, PEG MME 2000, DMSO |
