1E44
ribonuclease domain of colicin E3 in complex with its immunity protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Wavelength(s) | 0.9, 0.97, 0.979 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 93.700, 93.700, 76.170 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.192 |
| Rwork | 0.192 |
| R-free | 0.22800 |
| Structure solution method | MAD |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.860 |
| Data reduction software | DENZO |
| Data scaling software | SCALA |
| Phasing software | SOLVE |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.450 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.039 * | 0.237 * |
| Number of reflections | 14892 | |
| <I/σ(I)> | 37.8 | 2.8 |
| Completeness [%] | 98.7 | 97.5 |
| Redundancy | 3 | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 277 * | Carr, S., (1999) Acta Crystallogr., D56, 1630. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 45-50 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | reservoir | sodium citrate | 0.1 (M) | |
| 4 | 1 | reservoir | PEG4000 | 20 (%(v/v)) | |
| 5 | 1 | reservoir | 2-propanol | 20 (%(v/v)) |
