2HFP
Crystal Structure of PPAR Gamma with N-sulfonyl-2-indole carboxamide ligands
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 | CCD |
| Collection date | 2005-01-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.487, 77.178, 82.075 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.800 - 2.000 |
| R-factor | 0.209 |
| Rwork | 0.205 |
| R-free | 0.28500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.808 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.821 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.043 | 0.334 |
| Number of reflections | 19433 | |
| <I/σ(I)> | 16.83 | 3.48 |
| Completeness [%] | 93.4 | 72.8 |
| Redundancy | 0.93 | 0.73 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 298 | Two microliters of protein solution (10 mg/mL, 1 peptide fragment) was added to two microliters of well (2% Peg400, 1.6 Molar ammonium sulfate, 100 mM Mes 6.5) and hung over 1000 microliters well in a 2 + 2 hanging drop crystallization setup , temperature 298.0K |
