5P92
humanized rat catechol O-methyltransferase in complex with 5-(4-fluorophenyl)-2,3-dihydroxy-N-(4-thieno[2,3-c]pyridin-2-ylbutyl)benzamide at 1.61A
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 | 2010-02-04 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.999900 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 49.929, 54.207, 81.134 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.070 - 1.610 |
R-factor | 0.1722 |
Rwork | 0.170 |
R-free | 0.20640 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.019 |
RMSD bond angle | 1.825 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0041) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.070 | 45.070 | 1.650 |
High resolution limit [Å] | 1.610 | 7.200 | 1.610 |
Rmerge | 0.052 | 0.043 | 0.134 |
Rmeas | 0.057 | 0.048 | 0.155 |
Total number of observations | 178861 | ||
Number of reflections | 28907 | 393 | 1829 |
<I/σ(I)> | 21.93 | 32.48 | 6.9 |
Completeness [%] | 98.8 | 98.5 | 86 |
Redundancy | 6.19 | ||
CC(1/2) | 0.999 | 0.997 | 0.975 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 295 | AMMONIUM SULPHATE, CHES, PH 9 |