3A7D
Crystal Structures of rat Catechol-O-Methyltransferase complexed with new bi-substrate type inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL32B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-16 |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 50.075, 58.082, 79.198 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 10.000 - 2.400 |
| R-factor | 0.16601 |
| Rwork | 0.159 |
| R-free | 0.22466 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vid |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.181 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.800 | 2.530 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.072 | 0.218 |
| Number of reflections | 9468 | |
| <I/σ(I)> | 27.9 | 9.1 |
| Completeness [%] | 96.2 | 96.1 |
| Redundancy | 7.2 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 0.2M (NH4)2SO4, 0.1M Tris pH 7.5, 30% (w/v) PEG 400, 0.35% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
