1J12
Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 177.900, 112.900, 146.200 |
Unit cell angles | 90.00, 105.80, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.100 |
Rwork | 0.198 |
R-free | 0.25300 |
Starting model (for MR) | 5bca |
RMSD bond length | 0.007 |
RMSD bond angle | 21.965 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.400 | 2.090 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.087 | 0.247 |
Total number of observations | 257638 * | |
Number of reflections | 128094 | 6376 * |
Completeness [%] | 68.6 | 27.4 |
Redundancy | 2.0 * | 1.2 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 293 | Oyama, T., (1998) Protein Pept.Lett., 5, 349. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | ammonium chloride | 50 (mM) | |
3 | 1 | reservoir | PEG6000 | 6-8 (%(w/v)) | |
4 | 1 | reservoir | ammonium chloride | 50 (mM) |