2NXC
Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)
Experimental 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 | 2005-09-25 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9797 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 81.521, 76.557, 61.878 |
Unit cell angles | 90.00, 130.01, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.590 |
R-factor | 0.1939 |
Rwork | 0.192 |
R-free | 0.22405 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ufk |
RMSD bond length | 0.011 |
RMSD bond angle | 1.523 |
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 | 1.650 |
High resolution limit [Å] | 1.590 | 1.590 |
Rmerge | 0.057 | 0.385 |
Number of reflections | 37520 | |
<I/σ(I)> | 17.96 | 2.6 |
Completeness [%] | 96.2 | 91.2 |
Redundancy | 3 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | sitting-drop vapor diffusion and microseeding | 6.8 | 298 | 700mM ammonium sulfate, 4%v/v Dioxane, 220mM Hexanediol, 20mM MES, pH 6.8, sitting-drop vapor diffusion and microseeding, temperature 298K |