1MQE
Structure of the MT-ADPRase in complex with gadolidium and ADP-ribose, a Nudix enzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 93 |
Detector technology | IMAGE PLATE |
Collection date | 2001-11-20 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.54 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 64.052, 64.052, 182.212 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
Rwork | 0.205 |
R-free | 0.26600 |
Structure solution method | MIR |
RMSD bond length | 0.023 |
RMSD bond angle | 1.470 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.075 * | |
Total number of observations | 127268 * | |
Number of reflections | 15604 | |
<I/σ(I)> | 21.3 | |
Completeness [%] | 98.6 | 97.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | Sodium formate, Tris HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | pH7.5 |
3 | 1 | drop | EDTA | 1 (mM) | |
4 | 1 | reservoir | sodium formate | 4.3 (M) | |
5 | 1 | reservoir | Tris | 100 (mM) | pH8.0 |