1RI4
Structure and mechanism of mRNA cap (guanine N-7) methyltransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 63.803, 63.803, 112.683 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 * - 2.400 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.28000 * |
Structure solution method | SAD+MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 1.150 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.066 | 0.231 * |
Total number of observations | 124773 * | |
Number of reflections | 9398 | |
<I/σ(I)> | 26.4 | |
Completeness [%] | 86.5 | 64.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8 * | 291 | 1.2M Na/K tartrate, 50mM BIS/TRIS, 20mM DTT, pH 6.25, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6.5 (mg/ml) | |
2 | 1 | drop | 220 (mM) | ||
3 | 1 | drop | Tris-HCl | 20 (mM) | pH8.0 |
4 | 1 | drop | beta-mercaptoethanol | 1 (mM) | |
5 | 1 | reservoir | sodium/pootassium tartrate | 1.2 (M) | |
6 | 1 | reservoir | bis-tris | 50 (mM) | pH6.0 |
7 | 1 | reservoir | dithiothreitol | 20 (mM) |