8DKN
PPARg bound to T0070907 and Co-R peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 2016-03-19 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 0.9786 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 83.208, 81.890, 48.146 |
Unit cell angles | 90.00, 103.79, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.950 |
R-factor | 0.2299 |
Rwork | 0.227 |
R-free | 0.29730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2prg |
RMSD bond length | 0.015 |
RMSD bond angle | 1.816 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.020 |
High resolution limit [Å] | 1.950 | 4.200 | 1.950 |
Rmerge | 0.077 | 0.063 | 0.496 |
Rmeas | 0.090 | 0.075 | 0.592 |
Rpim | 0.047 | 0.040 | 0.318 |
Total number of observations | 84160 | ||
Number of reflections | 22981 | 2333 | 2270 |
<I/σ(I)> | 11.3 | ||
Completeness [%] | 99.8 | 99 | 100 |
Redundancy | 3.7 | 3.6 | 3.4 |
CC(1/2) | 0.987 | 0.929 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9.5 | 296 | 2+2 uL drops made from a 2:2:1 molar ratio of T007:NCOR peptide:PPARg and well solution containing 1.8-2.2 M (NH3)2SO4, 0.2 M Li2SO4 and 100 mM CAPS pH 9.5. Protein formulated at 20 mg mL-1 in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1mM TCEP |