3CJT
Ribosomal protein L11 methyltransferase (PrmA) in complex with dimethylated ribosomal protein L11
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-06-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9797 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 69.822, 69.943, 379.007 |
| Unit cell angles | 90.00, 90.47, 90.00 |
Refinement procedure
| Resolution | 29.740 - 2.300 |
| R-factor | 0.19765 |
| Rwork | 0.194 |
| R-free | 0.25930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 2NXC 2nxn |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.538 |
| 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 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.071 | 0.364 |
| Number of reflections | 157914 | |
| <I/σ(I)> | 25 | 2.7 |
| Completeness [%] | 96.5 | 76.7 |
| Redundancy | 6.7 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | microbatch under oil | 5.8 | 277 | 200mM magnesium nitrate hexahydrate, 20% w/v PEG3350, 4mM AdoMet, pH 5.8, microbatch under oil, temperature 277K |
