5SER
Crystal Structure of human phosphodiesterase 10 in complex with 4-N-(2-fluoroethyl)-4-N,2-dimethyl-3-N-(2-phenyl-[1,2,4]triazolo[1,5-a]pyridin-7-yl)pyrazole-3,4-dicarboxamide
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 | 2012-05-05 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999970 |
Spacegroup name | H 3 |
Unit cell lengths | 135.109, 135.109, 234.956 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.500 - 2.250 |
R-factor | 0.1753 |
Rwork | 0.172 |
R-free | 0.23290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.015 |
RMSD bond angle | 2.036 |
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] | 43.500 | 43.500 | 2.310 |
High resolution limit [Å] | 2.250 | 10.060 | 2.250 |
Rmerge | 0.056 | 0.013 | 1.110 |
Rmeas | 0.063 | 0.014 | 1.244 |
Total number of observations | 392973 | ||
Number of reflections | 75782 | 838 | 5516 |
<I/σ(I)> | 21.35 | 107.89 | 1.5 |
Completeness [%] | 99.9 | 98.8 | 99 |
Redundancy | 5.186 | 4.996 | 4.987 |
CC(1/2) | 1.000 | 1.000 | 0.622 |
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 |