8EOM
TUDOR DOMAIN OF TUMOR SUPPRESSOR P53BP1 WITH MFP-5973
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-07-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 43.523, 51.188, 105.601 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.270 - 1.700 |
| R-factor | 0.1986 |
| Rwork | 0.197 |
| R-free | 0.24360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g3r |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.489 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.8.2) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 4.610 | 1.700 |
| Rmerge | 0.062 | 0.029 | 0.758 |
| Rmeas | 0.073 | 0.034 | 0.881 |
| Rpim | 0.036 | 0.017 | 0.441 |
| Total number of observations | 102459 | ||
| Number of reflections | 26188 | 1448 | 1287 |
| <I/σ(I)> | 8.5 | ||
| Completeness [%] | 98.4 | 97.7 | 98.2 |
| Redundancy | 3.9 | 3.9 | 3.8 |
| CC(1/2) | 0.998 | 0.636 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 291 | 2M ammonium sulfate, 0.1 M HEPES pH 7.5, 2% PEG 400 |
