5SF3
Crystal Structure of human phosphodiesterase 10 in complex with 2-methyl-3-N-(2-phenylimidazo[1,2-a]pyrimidin-7-yl)-4-N-(1H-pyrazol-5-ylmethyl)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 | PIXEL |
Collection date | 2010-07-17 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 135.419, 135.419, 235.330 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.680 - 2.150 |
R-factor | 0.1741 |
Rwork | 0.172 |
R-free | 0.22360 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.016 |
RMSD bond angle | 2.093 |
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] | 43.680 | 43.680 | 2.210 |
High resolution limit [Å] | 2.150 | 9.620 | 2.150 |
Rmerge | 0.081 | 0.023 | 1.060 |
Rmeas | 0.090 | 0.025 | 1.174 |
Total number of observations | 461628 | ||
Number of reflections | 87515 | 968 | 6471 |
<I/σ(I)> | 14.6 | 60.02 | 1.67 |
Completeness [%] | 100.0 | 98.9 | 99.9 |
Redundancy | 5.275 | 5.211 | 5.413 |
CC(1/2) | 0.999 | 0.999 | 0.584 |
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 |