1GPJ
Glutamyl-tRNA Reductase from Methanopyrus kandleri
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-15 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 78.267, 98.650, 68.606 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 69.000 - 1.950 |
R-factor | 0.197 * |
Rwork | 0.212 |
R-free | 0.26000 * |
Structure solution method | MIR |
RMSD bond length | 0.030 * |
RMSD bond angle | 3.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.700 | 1.960 |
High resolution limit [Å] | 1.930 | 1.930 |
Rmerge | 0.073 | 0.324 |
Number of reflections | 32681 | |
<I/σ(I)> | 12 | 2.2 |
Completeness [%] | 91.1 | 69.1 |
Redundancy | 2.5 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 4 * | METHOD: HANGING DROP, TEMP.: 4C, PROTEIN CONCENTRATION: 9.8 MG/ML, PRECIPITANT: 30 MPD, BUFFER: 100MM HEPES PH 7.5, SALT: 200MM NACL, 200MM NACITRATE, 2MM MGCL2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 9.6 (mg/ml) | |
2 | 1 | reservoir | 0.2 (M) | ||
3 | 1 | reservoir | 2 (mM) | ||
4 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
5 | 1 | reservoir | sodium citrate | 0.2 (M) | |
6 | 1 | reservoir | MPD | 30 (%(v/v)) |