1GCY
HIGH RESOLUTION CRYSTAL STRUCTURE OF MALTOTETRAOSE-FORMING EXO-AMYLASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL24XU |
Synchrotron site | SPring-8 |
Beamline | BL24XU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-05-14 |
Detector | RIGAKU RAXIS IV |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 69.420, 171.660, 46.350 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.600 |
R-factor | 0.259 |
Rwork | 0.259 |
R-free | 0.30400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2amg |
RMSD bond length | 0.006 |
RMSD bond angle | 25.200 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.600 |
Rmerge | 0.061 |
Total number of observations | 222219 * |
Number of reflections | 66492 |
Completeness [%] | 89.6 |
Redundancy | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 | 4 * | ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25.7 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | reservoir | ammonium sulfate | 0.2 (M) |