5SK1
Crystal Structure of human phosphodiesterase 10 in complex with 4-N,2-dimethyl-3-N-(2-phenylimidazo[1,2-a]pyrimidin-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 | CCD |
Collection date | 2009-04-03 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.007500 |
Spacegroup name | H 3 |
Unit cell lengths | 134.851, 134.851, 234.435 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 41.370 - 2.300 |
R-factor | 0.1874 |
Rwork | 0.185 |
R-free | 0.23840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.008 |
RMSD bond angle | 1.505 |
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] | 41.370 | 41.370 | 2.360 |
High resolution limit [Å] | 2.300 | 10.290 | 2.300 |
Rmerge | 0.072 | 0.022 | 0.972 |
Rmeas | 0.083 | 0.026 | 1.130 |
Total number of observations | 274205 | ||
Number of reflections | 70543 | 752 | 5220 |
<I/σ(I)> | 13.72 | 51.63 | 1.46 |
Completeness [%] | 99.9 | 94.5 | 100 |
Redundancy | 3.887 | 3.632 | 3.865 |
CC(1/2) | 0.999 | 0.999 | 0.520 |
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 |