3ZXJ
Engineering the active site of a GH43 glycoside hydrolase generates a biotechnologically significant enzyme that displays both endo- xylanase and exo-arabinofuranosidase activity
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-12-04 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.318, 78.260, 95.767 |
| Unit cell angles | 90.00, 103.13, 90.00 |
Refinement procedure
| Resolution | 47.750 - 1.850 |
| R-factor | 0.15638 |
| Rwork | 0.155 |
| R-free | 0.18923 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.386 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.750 | 1.890 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.120 | 0.460 |
| Number of reflections | 80563 | |
| <I/σ(I)> | 13.8 | 5.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10.2 | 8.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 0.1 M BIS-TRIS PH 6.5, 22 % (W/V) PEG3350, 2 M AMMONIUM SULFATE |
