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. |