5SFX
Crystal Structure of human phosphodiesterase 10 in complex with N-(2-acetamido-1,3-benzothiazol-5-yl)-4-(azetidine-1-carbonyl)-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 | 2010-02-01 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999900 |
Spacegroup name | H 3 |
Unit cell lengths | 135.943, 135.943, 235.595 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.720 - 2.040 |
R-factor | 0.1788 |
Rwork | 0.176 |
R-free | 0.22250 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.016 |
RMSD bond angle | 2.012 |
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] | 43.720 | 43.720 | 2.090 |
High resolution limit [Å] | 2.040 | 9.120 | 2.040 |
Rmerge | 0.076 | 0.018 | 1.488 |
Rmeas | 0.085 | 0.020 | 1.668 |
Total number of observations | 536667 | ||
Number of reflections | 103327 | 1148 | 7685 |
<I/σ(I)> | 14.84 | 60.47 | 1.2 |
Completeness [%] | 100.0 | 99.2 | 99.9 |
Redundancy | 5.194 | 5.382 | 4.905 |
CC(1/2) | 0.999 | 1.000 | 0.459 |
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 |