1H12
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 | 50.972, 90.734, 97.581 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 1.200 |
R-factor | 0.108 |
Rwork | 0.107 |
R-free | 0.13020 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | WILD TYPE WITHOUT LIGAND |
RMSD bond length | 0.022 * |
RMSD bond angle | 1.586 * |
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 | 1.220 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.032 | 0.235 |
Total number of observations | 1757738 * | |
Number of reflections | 141707 | |
<I/σ(I)> | 43.52 | 3.69 |
Completeness [%] | 99.4 | 91.9 |
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 |