6VO5
Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4
Replaces: 6UHDExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-12-11 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97926 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 116.726, 155.636, 53.475 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.450 - 1.600 |
| R-factor | 0.1721 |
| Rwork | 0.171 |
| R-free | 0.19760 |
| Structure solution method | FOURIER SYNTHESIS |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.406 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 48.620 | 48.620 | 1.630 |
| High resolution limit [Å] | 1.600 | 8.760 | 1.600 |
| Rmerge | 0.059 | 0.025 | 1.066 |
| Rmeas | 0.062 | 0.027 | 1.129 |
| Rpim | 0.021 | 0.009 | 0.367 |
| Total number of observations | 1132308 | 7435 | 57634 |
| Number of reflections | 128467 | 903 | 6322 |
| <I/σ(I)> | 20.3 | 66.9 | 1.9 |
| Completeness [%] | 99.5 | 98.3 | 99.5 |
| Redundancy | 8.8 | 8.2 | 9.1 |
| CC(1/2) | 0.999 | 0.999 | 0.723 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 12% PEG 20K and 0.1M MES pH6.5 |
