1PXG
Crystal structure of the mutated tRNA-guanine transglycosylase (TGT) D280E complexed with preQ1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 103 |
Detector technology | IMAGE PLATE |
Collection date | 2002-11-06 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 91.280, 64.940, 70.200 |
Unit cell angles | 90.00, 96.12, 90.00 |
Refinement procedure
Resolution | 10.000 - 1.700 |
R-factor | 0.1594 |
Rwork | 0.159 |
R-free | 0.20600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pud |
RMSD bond length | 0.008 |
RMSD bond angle | 0.027 |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.067 | 0.253 |
Total number of observations | 155496 * | |
Number of reflections | 42492 | |
<I/σ(I)> | 24.3 | 6.1 |
Completeness [%] | 94.5 | 90.6 |
Redundancy | 3.6 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 25. * | Romier, C., (1996) Proteins: Struct.,Funct., Genet., 24, 516. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | Tris-HCl | 100 (mM) | |
2 | 1 | reservoir | PEG8000 | 13 (%) | |
3 | 1 | reservoir | dithiothreitol | 1 (mM) | |
4 | 1 | reservoir | agarose | 0.2 (%) | |
5 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
6 | 1 | drop | 2 (M) | ||
7 | 1 | drop | dithiothreitol | 1 (mM) | |
8 | 1 | drop | protein | 12 (mg/ml) |