7SMF
p107 pocket domain complexed with mutated HDAC1-3X peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-07-27 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.033 |
| Spacegroup name | P 1 |
| Unit cell lengths | 63.158, 63.302, 83.344 |
| Unit cell angles | 85.94, 68.44, 73.99 |
Refinement procedure
| Resolution | 39.290 - 3.000 |
| R-factor | 0.2392 |
| Rwork | 0.236 |
| R-free | 0.30140 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4yos |
| RMSD bond length | 0.014 |
| RMSD bond angle | 2.076 |
| Data reduction software | xia2 |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.17.1_3660: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.290 | 3.180 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.251 | 0.740 |
| Number of reflections | 21589 | 3425 |
| <I/σ(I)> | 3.1 | 1.3 |
| Completeness [%] | 93.5 | |
| Redundancy | 2 | |
| CC(1/2) | 0.810 | 0.640 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 100 mM MES, pH 6.5, 4% PEG400, 1.6 M ammonium sulfate |
