1JL8
Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 292 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-11-30 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 118.019, 120.359, 113.524 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.500 - 3.200 |
| R-factor | 0.189 * |
| Rwork | 0.189 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bvz |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.400 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 81.650 | 3.310 |
| High resolution limit [Å] | 3.200 | 3.200 |
| Rmerge | 0.077 | 0.269 |
| Total number of observations | 73577 * | |
| Number of reflections | 23296 | |
| <I/σ(I)> | 12.1 | |
| Completeness [%] | 85.1 | 87.4 |
| Redundancy | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 19 * | MES, methyl beta-cyclodextrin, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | PEG6000 | 2 (%(w/v)) | |
| 2 | 1 | reservoir | 5 (mM) | ||
| 3 | 1 | reservoir | MES | 40 (mM) | pH6.0 |
| 4 | 1 | drop | protein | 20 (mg/ml) |
