1E40
Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1994-10-15 |
Detector | RAXIS IIC |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 52.720, 78.270, 238.860 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.200 |
R-factor | 0.13 * |
Rwork | 0.130 |
R-free | 0.21000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1e3x |
RMSD bond length | 0.010 |
RMSD bond angle | 0.030 |
Data reduction software | DENZO |
Data scaling software | Agrovata |
Phasing software | CCP4 |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.300 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.050 | 0.089 * |
Number of reflections | 23662 | |
<I/σ(I)> | 33 | 13 |
Completeness [%] | 94.0 | 77 |
Redundancy | 5.2 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 18 * | CRYSTALS WERE GROWN AT 18C USING THE HANGING DROP METHOD WITH 8-13% MONOMETHYL ETHER POLYETHYLENE GLYCOL 2000 OR 5000 AS PRECIPITANT. DROPS WERE BUFFERED WITH 0.1M TRIS/HCL PH 7.5 CONTAINING 5MM CACL2 AND THE PROTEIN CONCENTRATION WAS 30-35MG/ML. CRYSTALS WERE THEN SOAKED IN 10MM MALTOTRIOSE SOLUTION TO OBTAIN THE COMPLEX. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | mmePEG2000 | 8-13 (%(w/v)) | or PEG5000 |
2 | 1 | drop | Tris-HCl | 0.1 (M) | |
3 | 1 | drop | 5 (mM) | ||
4 | 1 | drop | protein | 30-35 (M) |