8GQ4
Histone acetyltransferase Rtt109 mutant-N195A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL17U1 |
| Synchrotron site | SSRF |
| Beamline | BL17U1 |
| Temperature [K] | 126.15 |
| Detector technology | PIXEL |
| Collection date | 2017-08-03 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9754 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.768, 69.840, 54.585 |
| Unit cell angles | 90.00, 114.22, 90.00 |
Refinement procedure
| Resolution | 49.780 - 1.770 |
| R-factor | 0.1908 |
| Rwork | 0.188 |
| R-free | 0.23410 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7bxw |
| RMSD bond length | 0.012 |
| RMSD bond angle | 2.012 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.820 |
| High resolution limit [Å] | 1.770 | 1.770 |
| Rmerge | 0.185 | 0.335 |
| Number of reflections | 34445 | 2832 |
| <I/σ(I)> | 11.42 | |
| Completeness [%] | 100.0 | |
| Redundancy | 7.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 291.15 | 0.1 M Bis-Tris pH 6.0, 2% Tacsimate pH 6.0, 15~20% PEG 3350 |






