2P54
a crystal structure of PPAR alpha bound with SRC1 peptide and GW735
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-07-05 |
Detector | MAR CCD 165 mm |
Wavelength(s) | 1.00 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 61.263, 103.535, 49.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.790 |
R-factor | 0.204 |
Rwork | 0.204 |
R-free | 0.22700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | apo PPAR alpha |
RMSD bond length | 0.005 |
RMSD bond angle | 1.287 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.860 |
High resolution limit [Å] | 1.790 | 1.790 |
Rmerge | 0.045 | 0.350 |
Number of reflections | 30145 | |
<I/σ(I)> | 39.45 | 5.2 |
Completeness [%] | 98.0 | 95.8 |
Redundancy | 7.1 | 7.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 295 | 7% PEG 3350, 200 mM NaF, 12% 2,5-hexanediol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |