5LKZ
Crystal structure of the p300 acetyltransferase catalytic core with crotonyl-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 | 2015-08-28 |
Detector | DECTRIS PILATUS3 2M |
Wavelength(s) | 0.872600 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 93.600, 155.910, 110.090 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
R-factor | 0.20014 |
Rwork | 0.198 |
R-free | 0.23386 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4bhw |
RMSD bond length | 0.009 |
RMSD bond angle | 1.349 |
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 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmeas | 0.165 | 1.047 |
Number of reflections | 28182 | |
<I/σ(I)> | 9.93 | 1.81 |
Completeness [%] | 99.8 | 100 |
Redundancy | 6.2 | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277 | Tris, PEG MME 2000 |