5SF8
Crystal Structure of human phosphodiesterase 10 in complex with 4-(azetidine-1-carbonyl)-2-methyl-N-[2-(5-phenyl-2-pyridin-2-yl-1,2,4-triazol-3-yl)ethyl]pyrazole-3-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 | PIXEL |
Collection date | 2011-11-06 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999900 |
Spacegroup name | H 3 |
Unit cell lengths | 135.206, 135.206, 235.361 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.490 - 2.150 |
R-factor | 0.1738 |
Rwork | 0.171 |
R-free | 0.22540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.010 |
RMSD bond angle | 1.642 |
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] | 43.490 | 43.490 | 2.210 |
High resolution limit [Å] | 2.150 | 9.620 | 2.150 |
Rmerge | 0.088 | 0.018 | 1.137 |
Rmeas | 0.098 | 0.020 | 1.263 |
Total number of observations | 454445 | ||
Number of reflections | 87217 | 969 | 6457 |
<I/σ(I)> | 14.56 | 65.05 | 1.52 |
Completeness [%] | 99.9 | 99.1 | 100 |
Redundancy | 5.211 | 5.131 | 5.292 |
CC(1/2) | 0.999 | 1.000 | 0.526 |
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 |