1AQH
ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1996-12 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 71.400, 138.700, 115.700 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.000 - 2.000 |
R-factor | 0.157 |
Rwork | 0.157 |
R-free | 0.20400 |
Structure solution method | PHASES FROM ALPHA-AMYLASE COMPLEXED WITH A TRIS MOLECULE COMBINED WITH STRUCTURE FACTORS FROM THIS NATIVE DATA SET |
RMSD bond length | 0.008 |
RMSD bond angle | 1.184 * |
Data reduction software | DENZO |
Data scaling software | AGROVATA |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.142 * | 0.142 * |
Total number of observations | 93724 * | |
Number of reflections | 31485 | |
<I/σ(I)> | 5 | 1.1 |
Completeness [%] | 80.5 | 31.5 |
Redundancy | 3 | 1.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | Aghajari, N., (1996) Protein Sci., 5, 2128. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | MPD | 60-70 (%) | |
2 | 1 | reservoir | HEPES | 0.1 (M) |