1E3Z
Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-05-15 |
| Detector | MARRESEARCH |
| 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 - 1.930 |
| R-factor | 0.13 * |
| Rwork | 0.130 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e3x |
| RMSD bond length | 0.010 |
| RMSD bond angle | 0.026 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.960 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.070 | 0.130 |
| Number of reflections | 38273 | |
| <I/σ(I)> | 16 | 10 |
| Completeness [%] | 100.0 | 99 |
| Redundancy | 4.1 | 3.5 |
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 ACARBOSE 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) |
