1OY5
Crystal structure of tRNA (m1G37) methyltransferase from Aquifex aeolicus
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.2 |
Synchrotron site | ALS |
Beamline | 5.0.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-05-23 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9640,0.9793 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 153.351, 96.139, 57.426 |
Unit cell angles | 90.00, 96.24, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.28048 |
Rwork | 0.279 |
R-free | 0.30000 * |
Structure solution method | MAD |
RMSD bond length | 0.018 * |
RMSD bond angle | 1.970 * |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.640 |
High resolution limit [Å] | 2.580 | 2.580 |
Number of reflections | 31977 | |
Completeness [%] | 96.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 278 | Jancarik, J., (1991) J. Appl. Crystallogr., 24, 409. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | sodium cirtate | 0.1 (M) | pH5.5 |
3 | 1 | reservoir | PEG3000 | 20 (%) |