2NXN
T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4C |
| Synchrotron site | NSLS |
| Beamline | X4C |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-03-15 |
| Detector | MAR scanner 345 mm plate |
| Spacegroup name | P 65 |
| Unit cell lengths | 132.844, 132.844, 46.006 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.22273 |
| Rwork | 0.220 |
| R-free | 0.27277 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb entries 1MMS 2nxc |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.747 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | COMO |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.077 | 0.395 |
| Number of reflections | 18330 | |
| <I/σ(I)> | 17.6 | 2.8 |
| Completeness [%] | 98.9 | 96.9 |
| Redundancy | 4.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 25.5 % w/v PEG4000, 120 mM Sodium Acetate, 85mM TRIS, pH 8.5, 15 % v/v glycerol, 4% v/v 1,1,1,3,3,3-Hexafluoro-2-propanol, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
