5LKU
Crystal structure of the p300 acetyltransferase catalytic core with 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 | 2015-06-29 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.872600 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 93.960, 156.400, 110.680 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.010 - 3.500 |
| R-factor | 0.20248 |
| Rwork | 0.200 |
| R-free | 0.24223 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4bhw |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.390 |
| 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 | 3.590 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmeas | 0.383 | 1.128 |
| Number of reflections | 10571 | |
| <I/σ(I)> | 5.65 | 2.29 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 7.04 | 7.34 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | Tris, PEG MME 2000 |
