1REO
L-amino acid oxidase from Agkistrodon halys pallas
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 300 |
Wavelength(s) | 0.8883 |
Spacegroup name | I 21 3 |
Unit cell lengths | 169.310, 169.310, 169.310 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.310 |
R-factor | 0.194 |
Rwork | 0.194 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1f8r |
RMSD bond length | 0.006 |
RMSD bond angle | 22.400 * |
Data reduction software | AUTOMAR |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | |
High resolution limit [Å] | 2.310 * | 2.310 * |
Rmerge | 0.054 * | 0.383 * |
Total number of observations | 247448 * | |
Number of reflections | 34867 | |
Completeness [%] | 98.2 * | 99.8 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 300 | ammonium sulfate, citrate soldium, nikel sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 44 (mg/ml) | in double-distilled water |
2 | 1 | reservoir | sodium citrate | 0.1 (M) | pH5.6 |
3 | 1 | reservoir | ammonium sulfate | 2 (M) | |
4 | 1 | reservoir | 10 (mM) |