3AKQ
Crystal structure of xylanase from Trichoderma longibrachiatum
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL26B1 |
Synchrotron site | SPring-8 |
Beamline | BL26B1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2008-11-19 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.8 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.921, 37.516, 84.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.140 - 0.970 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.20400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1enx |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.000 |
High resolution limit [Å] | 0.970 | 0.970 |
Rmerge | 0.041 | 0.470 |
Number of reflections | 116654 | |
<I/σ(I)> | 12.7 | 3.5 |
Completeness [%] | 99.8 | 99.3 |
Redundancy | 6.7 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | oil microbatch | 6.5 | 293 | 18% PEG 8000, 0.2M zinc acetate, pH 6.5, oil microbatch, temperature 293K |