2ZLB
Crystal structure of APO form of rat catechol-O-methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL32B2 |
Synchrotron site | SPring-8 |
Beamline | BL32B2 |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2003-07-04 |
Detector | RIGAKU JUPITER 210 |
Wavelength(s) | 1.0 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 56.262, 56.262, 117.483 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.200 |
R-factor | 0.18159 |
Rwork | 0.179 |
R-free | 0.23747 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1vid |
RMSD bond length | 0.020 |
RMSD bond angle | 2.144 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.160 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.070 | 0.241 |
Number of reflections | 11356 | |
<I/σ(I)> | 20 | 7.5 |
Completeness [%] | 98.7 | 94.6 |
Redundancy | 7.2 | 7.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 0.2M (NH4)2SO4, 30% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |