5UY9
Prolyl isomerase Pin1 R14A mutant bound with Brd4 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 77.1 |
| Detector technology | CCD |
| Collection date | 2016-04-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 68.534, 68.534, 79.640 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.070 - 1.850 |
| R-factor | 0.2351 |
| Rwork | 0.232 |
| R-free | 0.29078 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Data reduction software | HKL-2000 (HKL2000) |
| Data scaling software | HKL-2000 (HKL2000) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 33.070 |
| High resolution limit [Å] | 1.850 |
| Number of reflections | 17865 |
| <I/σ(I)> | 5.48 |
| Completeness [%] | 96.9 |
| Redundancy | 9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 140 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4 , 1.8 mM KH2PO4, PH 7.3 |
