5SFL
Crystal Structure of human phosphodiesterase 10 in complex with 6-cyclopropyl-N-[5-[(2-hydroxy-2-methylpropyl)carbamoyl]-1-methylpyrazol-4-yl]-3-(pyrimidin-5-ylamino)pyrazine-2-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 | 2010-04-23 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 135.036, 135.036, 234.927 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.440 - 2.130 |
R-factor | 0.1887 |
Rwork | 0.187 |
R-free | 0.22730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.007 |
RMSD bond angle | 1.417 |
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] | 43.440 | 43.440 | 2.190 |
High resolution limit [Å] | 2.130 | 9.530 | 2.130 |
Rmerge | 0.077 | 0.024 | 1.297 |
Rmeas | 0.088 | 0.027 | 1.483 |
Total number of observations | 385910 | ||
Number of reflections | 89235 | 992 | 6582 |
<I/σ(I)> | 12.35 | 50.29 | 1.14 |
Completeness [%] | 99.9 | 98.5 | 99.8 |
Redundancy | 4.325 | 4.185 | 4.278 |
CC(1/2) | 0.999 | 0.999 | 0.399 |
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 |