1H14
Structure of a cold-adapted family 8 xylanase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 51.087, 90.891, 98.023 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 1.500 |
R-factor | 0.145 |
Rwork | 0.143 |
R-free | 0.17070 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | WILD TYPE |
RMSD bond length | 0.029 |
RMSD bond angle | 2.169 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CCP4 |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.064 | 0.267 |
Total number of observations | 479600 * | |
Number of reflections | 74080 | |
<I/σ(I)> | 16.21 | 2.57 |
Completeness [%] | 99.7 | 95.3 |
Redundancy | 5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 277 | Van Petegem, F., (2002) Acta Crystallogr., D58, 1494. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 2 (mg/ml) | |
2 | 1 | reservoir | MPD | 70 (%) | |
3 | 1 | reservoir | sodium acetate | 0.1 (M) | pH5.0 |