5SFG
Crystal Structure of human phosphodiesterase 10 in complex with N-[(3R)-1-(5-chloropyridin-2-yl)pyrrolidin-3-yl]-6-cyclopropyl-3-(pyrimidin-5-ylamino)pyridine-2-carboxamide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-10-12 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 136.146, 136.146, 235.981 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.790 - 2.310 |
R-factor | 0.1616 |
Rwork | 0.160 |
R-free | 0.19510 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.005 |
RMSD bond angle | 1.291 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 43.790 | 43.790 | 2.370 |
High resolution limit [Å] | 2.310 | 10.330 | 2.310 |
Rmerge | 0.131 | 0.082 | 0.536 |
Rmeas | 0.153 | 0.095 | 0.647 |
Total number of observations | 251346 | ||
Number of reflections | 70620 | 785 | 4565 |
<I/σ(I)> | 6.71 | 12.51 | 1.83 |
Completeness [%] | 98.7 | 98 | 86.1 |
Redundancy | 3.559 | 3.792 | 2.844 |
CC(1/2) | 0.984 | 0.983 | 0.554 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 295 | 5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2 |