3EGV
Ribosomal protein L11 methyltransferase (PrmA) in complex with trimethylated ribosomal protein L11
Replaces: 3CJUExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-15 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9797 |
| Spacegroup name | P 62 |
| Unit cell lengths | 134.547, 134.547, 48.944 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.750 |
| R-factor | 0.18416 |
| Rwork | 0.183 |
| R-free | 0.21332 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 2NXC 2nxn |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.503 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.810 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.056 | 0.334 |
| Number of reflections | 48051 | |
| <I/σ(I)> | 12.2 | 2 |
| Completeness [%] | 97.2 | 93.8 |
| Redundancy | 1.7 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | microbatch technique under oil | 6.5 | 277 | 160 mM calcium acetate hydrate, 80 mM sodium cacodylate, 14.4% w/v PEG8000, 20% v/v glycerol, 4mM AdoMet, pH 6.5, microbatch technique under oil, temperature 277.0K |






