5SF0
Crystal Structure of human phosphodiesterase 10 in complex with 4-(azetidine-1-carbonyl)-2-methyl-N-(3-pyridin-2-yl-1H-pyrazol-5-yl)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 | CCD |
Collection date | 2009-03-30 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 134.588, 134.588, 234.418 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.500 - 2.100 |
R-factor | 0.1994 |
Rwork | 0.197 |
R-free | 0.24210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.007 |
RMSD bond angle | 1.436 |
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] | 43.500 | 43.500 | 2.150 |
High resolution limit [Å] | 2.100 | 9.390 | 2.100 |
Rmerge | 0.110 | 0.032 | 1.247 |
Rmeas | 0.129 | 0.037 | 1.473 |
Total number of observations | 347743 | ||
Number of reflections | 92032 | 1024 | 6786 |
<I/σ(I)> | 7.78 | 24.07 | 1.08 |
Completeness [%] | 99.6 | 98.6 | 98.8 |
Redundancy | 3.779 | 3.739 | 3.6 |
CC(1/2) | 0.995 | 0.998 | 0.326 |
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 |