1ANG
CRYSTAL STRUCTURE OF HUMAN ANGIOGENIN REVEALS THE STRUCTURAL BASIS FOR ITS FUNCTIONAL DIVERGENCE FROM RIBONUCLEASE
Experimental procedure
Spacegroup name | C 2 2 21 |
Unit cell lengths | 83.400, 120.600, 37.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.400 |
R-factor | 0.22 |
Rwork | 0.220 |
RMSD bond length | 0.015 |
RMSD bond angle | 3.510 |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.400 * |
Rmerge | 0.110 * |
Total number of observations | 41725 * |
Number of reflections | 7229 * |
Completeness [%] | 88.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 5.2 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | sodium citrate | 0.01 (M) | |
3 | 1 | reservoir | sodium potassium tartrate | 0.2 (M) | |
4 | 1 | reservoir | PEG6000 | 20-25 (%) | |
5 | 1 | reservoir | beta-octyl glucoside | 0.5 (%) | |
6 | 1 | reservoir | sodium citrate | 0.01 (M) |