3BEJ
Structure of human FXR in complex with MFA-1 and co-activator peptide
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-02-28 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.98793, 0.97931, 0.97907, 0.96863 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.642, 90.889, 129.651 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.650 - 1.900 |
| R-factor | 0.203 |
| Rwork | 0.200 |
| R-free | 0.25400 |
| Structure solution method | MAD |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.271 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHARP |
| Refinement software | TNT |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.970 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.065 | 0.577 |
| Number of reflections | 41792 | |
| <I/σ(I)> | 10.7 | |
| Completeness [%] | 100.0 | 100 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 16-22% PEG3350, 0.1M Bis-Tris, 4 mM YCl(3), 0.2M Ammonium acetate, 1 mM DTT. Protein was carboxymethylated with iodoacetic acid, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
