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) |
