3RLA
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 RAXIS II |
Spacegroup name | P 32 |
Unit cell lengths | 89.000, 89.000, 115.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.540 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.28200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | RAT LIVER ARGINASE |
RMSD bond length | 0.013 |
RMSD bond angle | 24.300 * |
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] | 8.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.540 |
Rmerge | 0.105 | 0.400 |
Total number of observations | 65410 * | |
Number of reflections | 26381 | |
<I/σ(I)> | 4.3 | 3.9 |
Completeness [%] | 74.0 | 79.5 |
Redundancy | 2.5 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8.5 | 4 * | 12 - 18% PEG 8000, 50 MM BICINE PH = 8.5, 0.05% AZIDE, 1 MM MNCL2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 3-4 (mg/ml) | |
2 | 1 | drop | Bicine | 50 (mM) | |
3 | 1 | drop | PEG8000 | 7-8 (%) | |
4 | 1 | drop | sodium azide | 0.025 (%) | |
5 | 1 | drop | 0.5 (mM) | ||
6 | 1 | reservoir | Bicine | 50 (mM) | |
7 | 1 | reservoir | PEG8000 | 14-16 (%) | |
8 | 1 | reservoir | sodium azide | 0.05 (%) | |
9 | 1 | reservoir | 1 (mM) |