1E43
Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-09-15 |
| Detector | ADSC-Q4 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 52.200, 76.100, 236.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| R-factor | 0.133 * |
| Rwork | 0.133 |
| R-free | 0.18500 |
| 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 | 1.760 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.070 | 0.081 |
| Number of reflections | 51292 | |
| <I/σ(I)> | 15 | 13 |
| Completeness [%] | 98.0 | 99 |
| Redundancy | 3 | 3.1 |
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. |
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) |
