5SI1
Crystal Structure of human phosphodiesterase 10 in complex with 2-methyl-4-(morpholine-4-carbonyl)-N-(2-phenylimidazo[1,2-a]pyridin-7-yl)pyrazole-3-carboxamide, space group I23
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 | 2009-02-02 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.999900 |
Spacegroup name | I 2 3 |
Unit cell lengths | 142.221, 142.221, 142.221 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.040 - 1.750 |
R-factor | 0.176 |
Rwork | 0.175 |
R-free | 0.20100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.003 |
RMSD bond angle | 1.199 |
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] | 44.970 | 38.040 | 1.800 |
High resolution limit [Å] | 1.750 | 7.830 | 1.750 |
Rmerge | 0.088 | 0.043 | 0.964 |
Rmeas | 0.098 | 0.048 | 1.067 |
Total number of observations | 262447 | ||
Number of reflections | 47955 | 485 | 3538 |
<I/σ(I)> | 9.71 | 20.28 | 1.52 |
Completeness [%] | 99.6 | 81.4 | 99.9 |
Redundancy | 5.473 | 4.687 | 5.523 |
CC(1/2) | 0.997 | 0.996 | 0.612 |
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 |