3D6E
Crystal structure of the engineered 1,3-1,4-beta-glucanase protein from Bacillus licheniformis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 |
| Unit cell lengths | 39.551, 54.813, 54.910 |
| Unit cell angles | 61.38, 85.72, 86.10 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.21259 |
| Rwork | 0.210 |
| R-free | 0.25481 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gbg |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.093 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.490 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.043 | 0.121 |
| Number of reflections | 14739 | |
| <I/σ(I)> | 18.7 | 6.25 |
| Completeness [%] | 93.5 | 79.2 |
| Redundancy | 1.8 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 16% PEG MME 2000, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
