5SHA
Crystal Structure of human phosphodiesterase 10 in complex with 2-[2-[5-[3-(difluoromethyl)pyrrolidin-1-yl]-2-methyl-1,2,4-triazol-3-yl]ethyl]-5,8-dimethyl-[1,2,4]triazolo[1,5-a]pyrazine
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 | 2013-03-17 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 134.647, 134.647, 235.144 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.320 - 2.240 |
R-factor | 0.1716 |
Rwork | 0.169 |
R-free | 0.22520 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.012 |
RMSD bond angle | 1.731 |
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] | 43.320 | 43.320 | 2.300 |
High resolution limit [Å] | 2.240 | 10.020 | 2.240 |
Rmerge | 0.082 | 0.017 | 1.234 |
Rmeas | 0.091 | 0.018 | 1.373 |
Total number of observations | 396216 | ||
Number of reflections | 76396 | 845 | 5644 |
<I/σ(I)> | 15.1 | 72 | 1.35 |
Completeness [%] | 99.9 | 98.9 | 100 |
Redundancy | 5.186 | 5.082 | 5.232 |
CC(1/2) | 0.999 | 1.000 | 0.523 |
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 |