3ZXL
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 |
| Collection date | 2009-05-25 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 65.310, 83.930, 97.890 |
| Unit cell angles | 90.00, 102.81, 90.00 |
Refinement procedure
| Resolution | 48.266 - 1.871 |
| R-factor | 0.1416 |
| Rwork | 0.139 |
| R-free | 0.18700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3zxj |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.555 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.270 | 1.890 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.090 | 0.170 |
| Number of reflections | 89446 | |
| <I/σ(I)> | 21.4 | 9.8 |
| Completeness [%] | 99.6 | 99.4 |
| Redundancy | 6.4 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | 0.1 M BIS-TRIS PROPANE PH 8.5, 20% (W/V) PEG3350, 0.2 M NAF. |
