3FS1
Crystal structure of HNF4a LBD in complex with the ligand and the coactivator PGC-1a fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2008-11-14 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 42 2 2 |
| Unit cell lengths | 113.049, 113.049, 57.322 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.200 |
| R-factor | 0.195 |
| Rwork | 0.190 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1PZL (without the ligand and the peptide) |
| RMSD bond length | 0.036 |
| RMSD bond angle | 2.444 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.200 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.090 | 0.349 |
| Number of reflections | 18995 | |
| <I/σ(I)> | 29.4 | 4.56 |
| Completeness [%] | 98.4 | 87 |
| Redundancy | 10.7 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
