9M4R
crystal structure of Arabidopsis thaliana ING1 PHD finger in complex with an H3K4me3 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-01-02 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.2824 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 41.830, 41.830, 69.435 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.226 - 1.700 |
| R-factor | 0.1586 |
| Rwork | 0.157 |
| R-free | 0.19970 |
| Structure solution method | SAD |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.712 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 3.660 | 1.700 |
| Rmerge | 0.090 | 0.075 | 0.220 |
| Rmeas | 0.077 | 0.227 | |
| Rpim | 0.018 | 0.054 | |
| Number of reflections | 8189 | 905 | 813 |
| <I/σ(I)> | 11.6 | ||
| Completeness [%] | 99.9 | 99.8 | 100 |
| Redundancy | 18.2 | 17.6 | 17.8 |
| CC(1/2) | 0.991 | 0.997 | 0.991 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | 40% PEG400, 5% PEG3000, and 0.1M MES, pH 6.0 |






