5SKU
Crystal Structure of human phosphodiesterase 10 in complex with 3-[4-[2-[2-(2-ethoxy-4-fluorophenyl)-5-methyl-1,3-oxazol-4-yl]ethoxy]naphthalen-1-yl]-2-methoxypropanoic acid
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 | 2010-09-19 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | H 3 |
Unit cell lengths | 135.289, 135.289, 234.535 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.550 - 2.200 |
R-factor | 0.1834 |
Rwork | 0.181 |
R-free | 0.22500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.007 |
RMSD bond angle | 1.401 |
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] | 43.550 | 43.550 | 2.260 |
High resolution limit [Å] | 2.200 | 9.840 | 2.200 |
Rmerge | 0.119 | 0.019 | 1.402 |
Rmeas | 0.132 | 0.021 | 1.559 |
Total number of observations | 426825 | ||
Number of reflections | 81260 | 905 | 6070 |
<I/σ(I)> | 13.35 | 65.36 | 1.2 |
Completeness [%] | 100.0 | 99 | 100 |
Redundancy | 5.253 | 5.22 | 5.261 |
CC(1/2) | 0.997 | 0.999 | 0.441 |
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 |