5SFT
Crystal Structure of human phosphodiesterase 10 in complex with 5,8-dimethyl-2-[2-(1-methyl-5-pyrrolidin-1-yl-1,2,4-triazol-3-yl)ethyl]-[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 | 2012-02-05 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999980 |
Spacegroup name | H 3 |
Unit cell lengths | 135.113, 135.113, 235.547 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.700 - 2.320 |
R-factor | 0.1786 |
Rwork | 0.176 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.008 |
RMSD bond angle | 1.466 |
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] | 43.700 | 43.700 | 2.380 |
High resolution limit [Å] | 2.320 | 10.380 | 2.320 |
Rmerge | 0.074 | 0.018 | 1.106 |
Rmeas | 0.083 | 0.020 | 1.227 |
Total number of observations | 361730 | ||
Number of reflections | 69397 | 767 | 5133 |
<I/σ(I)> | 15.18 | 63.75 | 1.43 |
Completeness [%] | 100.0 | 98.8 | 99.9 |
Redundancy | 5.212 | 5.056 | 5.289 |
CC(1/2) | 0.999 | 1.000 | 0.536 |
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 |