5SES
Crystal Structure of human phosphodiesterase 10 in complex with 4-(azetidine-1-carbonyl)-2-methyl-N-(2-phenyl-5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-7-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 | PIXEL |
Collection date | 2010-02-01 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999900 |
Spacegroup name | H 3 |
Unit cell lengths | 135.496, 135.496, 235.556 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.590 - 2.110 |
R-factor | 0.1752 |
Rwork | 0.172 |
R-free | 0.23050 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.016 |
RMSD bond angle | 2.106 |
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] | 43.590 | 43.590 | 2.160 |
High resolution limit [Å] | 2.110 | 9.440 | 2.110 |
Rmerge | 0.085 | 0.020 | 0.885 |
Rmeas | 0.096 | 0.023 | 0.985 |
Total number of observations | 446938 | ||
Number of reflections | 90072 | 1035 | 6852 |
<I/σ(I)> | 14.49 | 56 | 1.77 |
Completeness [%] | 97.1 | 99 | 100 |
Redundancy | 4.962 | 5.443 | 5.159 |
CC(1/2) | 0.998 | 0.999 | 0.683 |
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 |