3AKP
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 | 2010-01-28 |
Detector | RIGAKU RAXIS V |
Wavelength(s) | 0.8000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 56.657, 38.831, 81.254 |
Unit cell angles | 90.00, 94.78, 90.00 |
Refinement procedure
Resolution | 22.830 - 1.200 |
R-factor | 0.181 |
Rwork | 0.181 |
R-free | 0.19600 |
Structure solution method | FOURIER SYNTHESIS |
RMSD bond length | 0.011 |
RMSD bond angle | 1.400 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.240 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.087 | 0.495 |
Number of reflections | 105854 | |
<I/σ(I)> | 6.8 | 3 |
Completeness [%] | 95.5 | 89.8 |
Redundancy | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | oil microbatch | 8.5 | 293 | 30% PEG 4000, 0.2M sodium acetate, pH 8.5, oil microbatch, temperature 293K |