5RLA
ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1995-01 |
Detector | RIGAKU |
Spacegroup name | P 32 |
Unit cell lengths | 88.900, 88.900, 105.100 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.740 |
R-factor | 0.175 |
Rwork | 0.175 |
R-free | 0.27000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | RAT LIVER ARGINASE |
RMSD bond length | 0.012 |
RMSD bond angle | 24.400 * |
Data reduction software | MOSFLM |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.770 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.091 | 0.450 |
Total number of observations | 37872 * | |
Number of reflections | 23414 * | |
<I/σ(I)> | 5.2 | 1.5 |
Completeness [%] | 91.8 | 94.9 |
Redundancy | 1.6 | 1.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | 12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2 SOAKED FOR 1 WEEK IN 15MM EDTA + DPA |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16 (mg/ml) | |
2 | 1 | drop | bicine | 50 (mM) | |
3 | 1 | drop | 1 (mM) | ||
4 | 1 | reservoir | PEG8000 | 14 (%(w/v)) | |
5 | 1 | reservoir | bicine | 50 (mM) | |
6 | 1 | reservoir | 1 (mM) | ||
7 | 1 | reservoir | sodium azide | 0.05 (%(w/v)) |