3ZXK
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 | APS |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-25 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.380, 52.970, 146.870 |
| Unit cell angles | 90.00, 101.69, 90.00 |
Refinement procedure
| Resolution | 33.680 - 1.440 |
| R-factor | 0.16853 |
| Rwork | 0.166 |
| R-free | 0.20725 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zxj |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.476 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 33.680 | 1.470 |
| High resolution limit [Å] | 1.440 | 1.440 |
| Rmerge | 0.080 | 0.170 |
| Number of reflections | 177611 | |
| <I/σ(I)> | 16.2 | 9.8 |
| Completeness [%] | 99.2 | 98.3 |
| Redundancy | 2.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 0.1 M HEPES PH 7.5 22.5 % (W/V) PEG4000 0.1 M NACL |
