5SF1
Crystal Structure of human phosphodiesterase 10 in complex with 2-(difluoromethyl)-3-methyl-6-[2-(1-methyl-4-phenylimidazol-2-yl)ethynyl]imidazo[1,2-b]pyridazine
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 | 2011-12-11 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999910 |
Spacegroup name | H 3 |
Unit cell lengths | 135.436, 135.436, 235.715 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.740 - 2.110 |
R-factor | 0.1861 |
Rwork | 0.184 |
R-free | 0.23060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.010 |
RMSD bond angle | 1.668 |
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] | 43.740 | 43.740 | 2.160 |
High resolution limit [Å] | 2.110 | 9.440 | 2.110 |
Rmerge | 0.058 | 0.013 | 1.097 |
Rmeas | 0.067 | 0.015 | 1.252 |
Total number of observations | 404739 | ||
Number of reflections | 92694 | 1031 | 6894 |
<I/σ(I)> | 16.57 | 75.92 | 1.3 |
Completeness [%] | 99.9 | 98.7 | 99.9 |
Redundancy | 4.366 | 4.445 | 4.359 |
CC(1/2) | 0.999 | 1.000 | 0.462 |
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 |