1OPC
OMPR DNA-BINDING DOMAIN, ESCHERICHIA COLI
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-06 |
| Detector | FUJI |
| Wavelength(s) | 0.9686, 0.9876 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 59.140, 59.140, 58.110 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 5.000 - 1.950 |
| R-factor | 0.228 * |
| Rwork | 0.228 |
| R-free | 0.26900 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 0.036 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MADSYS |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.046 * | 0.086 * |
| Number of reflections | 8604 | |
| <I/σ(I)> | 10.8 | 6.9 |
| Completeness [%] | 97.1 | 98.7 |
| Redundancy | 7.1 | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.5 | 4 * | drop solution was mixed with an equal volume of reservoir solution * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20-25 (mg/ml) | |
| 2 | 1 | drop | betaME | 2 (mM) | |
| 3 | 1 | reservoir | PMME5000 | 3 (%) | |
| 4 | 1 | reservoir | MPD | 2.5 (%) | |
| 5 | 1 | reservoir | ethyleneglycol | 17.5 (%) | |
| 6 | 1 | reservoir | MES | 30 (mM) |
