5SFQ
Crystal Structure of human phosphodiesterase 10 in complex with 4-(azetidine-1-carbonyl)-N-[1-(2,2-difluoroethyl)pyrazol-3-yl]-2-methylpyrazole-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 | 2010-08-16 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.700000 |
Spacegroup name | H 3 |
Unit cell lengths | 134.458, 134.458, 234.587 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.260 - 2.210 |
R-factor | 0.1891 |
Rwork | 0.186 |
R-free | 0.24790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.012 |
RMSD bond angle | 1.811 |
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] | 43.260 | 43.260 | 2.270 |
High resolution limit [Å] | 2.210 | 9.880 | 2.210 |
Rmerge | 0.144 | 0.019 | 1.396 |
Rmeas | 0.160 | 0.022 | 1.549 |
Total number of observations | 418141 | ||
Number of reflections | 79123 | 880 | 5842 |
<I/σ(I)> | 11.85 | 60.39 | 1.17 |
Completeness [%] | 99.9 | 98.9 | 99.9 |
Redundancy | 5.285 | 5.105 | 5.324 |
CC(1/2) | 0.996 | 1.000 | 0.420 |
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 |