5P9X
humanized rat catechol O-methyltransferase in complex with N-[1-[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]propan-2-yl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide
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 | P 21 21 21 |
Unit cell lengths | 49.964, 54.087, 80.776 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.490 - 1.120 |
R-factor | 0.1607 |
Rwork | 0.160 |
R-free | 0.18400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.019 |
RMSD bond angle | 1.855 |
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] | 42.490 | 42.490 | 1.150 |
High resolution limit [Å] | 1.120 | 5.010 | 1.120 |
Rmerge | 0.082 | 0.043 | 0.927 |
Rmeas | 0.090 | 0.047 | 1.047 |
Total number of observations | 498356 | ||
Number of reflections | 83535 | 1081 | 5181 |
<I/σ(I)> | 10.17 | 27.88 | 1.37 |
Completeness [%] | 98.4 | 99.4 | 83.4 |
Redundancy | 5.97 | ||
CC(1/2) | 0.998 | 0.998 | 0.449 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 295 | AMMONIUM SULPHATE, CHES, PH 9 |