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 |