1A2V
COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Experimental procedure
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1995-12 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 138.770, 148.220, 234.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 - 2.400 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.22400 |
Structure solution method | MOLECULAR REPLACEMENT AND SIR |
Starting model (for MR) | 1oac |
RMSD bond length | 0.011 |
RMSD bond angle | 27.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEIT |
Phasing software | X-PLOR (3.843) |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.550 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.053 | 0.247 |
Number of reflections | 172832 | |
<I/σ(I)> | 12.5 | 2.4 |
Completeness [%] | 87.2 | 66.8 |
Redundancy | 2.8 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 6.5 * | PROTEIN WAS CRYSTALLIZED IN SITTING DROPS FROM 7-9% PEG 8000 AND 0.3 M POTASSIUM PHOSPHATE BUFFER, PH 6.2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | potassium phosphate | 155 (mM) | |
3 | 1 | drop | PEG8000 | 3.5-4.5 (%) | |
4 | 1 | reservoir | potassium phosphate | 0.3 (M) | |
5 | 1 | reservoir | PEG8000 | 7-9 (%) |