1E0W
Xylanase 10A from Sreptomyces lividans. native structure at 1.2 angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, Hamburg |
Beamline | X31 |
Temperature [K] | 297 |
Collection date | 1997-11-15 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.250, 46.930, 86.390 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.200 |
R-factor | 0.09 * |
Rwork | 0.098 |
R-free | 0.12400 |
Structure solution method | OTHER |
RMSD bond length | 0.010 |
RMSD bond angle | 0.025 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.220 |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.051 | 0.350 |
Number of reflections | 84936 | |
<I/σ(I)> | 23.6 | 3.4 |
Completeness [%] | 96.0 | 91 |
Redundancy | 4.3 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 4.6 | Derewenda, U., (1994) J.Biol.Chem., 269, 20811. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 60 (mg/ml) | |
2 | 1 | drop | PEG4000 | 5 (%) | |
3 | 1 | drop | sodium acetate | 100 (mM) | |
4 | 1 | reservoir | PEG4000 | 5 (%) | |
5 | 1 | reservoir | sodium acetate | 100 (mM) |