8DSY
PPARg bound to inverse agonist H3B-343
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Collection date | 2017-08-20 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | .9786 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 91.758, 63.503, 118.333 |
| Unit cell angles | 90.00, 101.40, 90.00 |
Refinement procedure
| Resolution | 49.510 - 2.950 |
| R-factor | 0.2032 |
| Rwork | 0.198 |
| R-free | 0.26690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2prg |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.470 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.000 |
| High resolution limit [Å] | 2.950 | 8.000 | 2.950 |
| Rmerge | 0.088 | 0.025 | 0.961 |
| Rmeas | 0.098 | 0.029 | 1.090 |
| Rpim | 0.044 | 0.013 | 0.506 |
| Total number of observations | 70991 | ||
| Number of reflections | 14263 | 742 | 679 |
| <I/σ(I)> | 8.8 | ||
| Completeness [%] | 99.9 | 99.1 | 99.3 |
| Redundancy | 5 | 4.6 | 4.6 |
| CC(1/2) | 0.999 | 0.748 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 296 | 2+2 uL drops of protein + reservoir consisting of 0.9-1.2 M Na citrate and 100 mM Tris pH 8.0. Protein formulated at 20 mg mL-1 in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1mM TCEP |
