5LKT
Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-26 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.976250 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 92.480, 154.690, 109.230 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.010 - 2.040 |
| R-factor | 0.17835 |
| Rwork | 0.177 |
| R-free | 0.20368 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bhw |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.304 |
| 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] | 50.010 | 2.090 |
| High resolution limit [Å] | 2.040 | 2.040 |
| Rmeas | 0.098 | 0.999 |
| Number of reflections | 49903 | |
| <I/σ(I)> | 12.65 | 2 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 5.5 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | Tris, PEG MME 2000 |
