1BAG
ALPHA-AMYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH MALTOPENTAOSE
Experimental procedure
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE BL-6A |
Synchrotron site | Photon Factory |
Beamline | BL-6A |
Temperature [K] | 288 |
Detector technology | IMAGE PLATE |
Collection date | 1995-10 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.590, 74.060, 117.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.500 |
R-factor | 0.198 |
Rwork | 0.198 |
R-free | 0.25200 |
Structure solution method | MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 24.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.610 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.067 * | 0.190 |
Total number of observations | 56354 * | |
Number of reflections | 18097 * | |
<I/σ(I)> | 16 | 5 |
Completeness [%] | 80.4 | 44 |
Redundancy | 2.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 10% PEG 3350, 3.5 MM CALCIUM CHLORIDE, 10 MM TRIS/HCL, PH 7.5. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 16.4 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | 3.5 (mM) | ||
4 | 1 | drop | acarbose | 2 (%) | |
5 | 1 | drop | G5 | 0.09-1.23 (%) | |
6 | 1 | reservoir | PEG3350 | 10 (%) |