1BVZ
ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 113 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-15 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 114.600, 117.900, 114.000 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.600 |
R-factor | 0.196 |
Rwork | 0.196 |
R-free | 0.27200 |
Structure solution method | MIRAS |
RMSD bond length | 0.012 |
RMSD bond angle | 2.800 |
Data scaling software | CCP4 |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.730 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.079 | 0.286 |
Total number of observations | 91759 * | |
Number of reflections | 43840 | |
<I/σ(I)> | 5.31 | 1.9 |
Completeness [%] | 91.8 | 78.1 |
Redundancy | 2.1 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.1 | 11 * | pH 6.1 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 2 (%(w/v)) | |
2 | 1 | reservoir | 2.5 (mM) | ||
3 | 1 | reservoir | MES | 20 (mM) | pH6.1 |
4 | 1 | drop | protein | 20 (mg/ml) |