8E6O
Crystal structure of human GCN5 histone acetyltransferase domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 80 |
| Detector technology | CCD |
| Collection date | 2021-06-13 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | I 4 2 2 |
| Unit cell lengths | 137.889, 137.889, 154.875 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.600 - 2.370 |
| R-factor | 0.2075 |
| Rwork | 0.205 |
| R-free | 0.24240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5trl |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.531 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.410 |
| High resolution limit [Å] | 2.370 | 6.430 | 2.370 |
| Rmerge | 0.083 | 0.030 | 0.770 |
| Rmeas | 0.086 | 0.032 | 0.807 |
| Rpim | 0.024 | 0.009 | 0.239 |
| Total number of observations | 385378 | ||
| Number of reflections | 30628 | 1669 | 1523 |
| <I/σ(I)> | 9.4 | ||
| Completeness [%] | 100.0 | 99.6 | 100 |
| Redundancy | 12.6 | 13.2 | 11.4 |
| CC(1/2) | 1.000 | 0.864 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 1 M Succinic acid pH 7.0, 0.1 M HEPES pH 7, and 1% w/v PEG MME 2000 |
