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 |