5SFO
Crystal Structure of human phosphodiesterase 10 in complex with 4-(azetidine-1-carbonyl)-2-methyl-N-[2-(1-methyl-4-phenylimidazol-2-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 | 2011-05-14 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 135.004, 135.004, 234.814 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.580 - 1.960 |
R-factor | 0.1779 |
Rwork | 0.176 |
R-free | 0.21770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.012 |
RMSD bond angle | 1.703 |
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] | 43.580 | 43.580 | 2.010 |
High resolution limit [Å] | 1.960 | 8.770 | 1.960 |
Rmerge | 0.107 | 0.036 | 1.269 |
Rmeas | 0.117 | 0.039 | 1.411 |
Total number of observations | 585272 | ||
Number of reflections | 113397 | 1273 | 8485 |
<I/σ(I)> | 7.29 | 29.42 | 1.35 |
Completeness [%] | 99.0 | 99.2 | 100 |
Redundancy | 4.71 | 5.592 | 5.267 |
CC(1/2) | 0.997 | 0.999 | 0.541 |
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 |