2Q6Z
Uroporphyrinogen Decarboxylase G168R single mutant apo-enzyme
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2003-09-16 |
Detector | RIGAKU RAXIS II |
Wavelength(s) | 1.5418 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 103.236, 103.236, 72.398 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 40.000 - 2.000 |
R-factor | 0.176 |
Rwork | 0.174 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1uro |
RMSD bond length | 0.015 |
RMSD bond angle | 1.416 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.109 | 0.497 |
Number of reflections | 30032 | |
<I/σ(I)> | 10.1 | |
Completeness [%] | 98.9 | 99 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 298 | Protein at 6.5 mg/ml in 50mM Tris, pH 7.5, 1mM BME was mixed 5 parts to 3 parts of precipitant (1.7M citrate, pH 7.0), VAPOR DIFFUSION, SITTING DROP, temperature 298K |