5VBT
Crystal structure of a highly specific and potent USP7 ubiquitin variant inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-16 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97891 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.011, 30.830, 51.046 |
| Unit cell angles | 90.00, 97.26, 90.00 |
Refinement procedure
| Resolution | 50.010 - 1.510 |
| R-factor | 0.1616 |
| Rwork | 0.160 |
| R-free | 0.18990 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ap4 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.442 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.530 |
| High resolution limit [Å] | 1.500 | 4.070 | 1.500 |
| Rmerge | 0.085 | 0.067 | 0.535 |
| Rmeas | 0.094 | 0.074 | 0.602 |
| Rpim | 0.040 | 0.031 | 0.268 |
| Total number of observations | 119284 | ||
| Number of reflections | 22616 | 1147 | |
| <I/σ(I)> | 5.9 | ||
| Completeness [%] | 98.8 | 97.1 | 97.4 |
| Redundancy | 5.3 | 5.2 | 4.5 |
| CC(1/2) | 0.995 | 0.792 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 1.2 M sodium citrate, 0.1 M Tris pH 8.5 |
