1B31
XYLANASE FROM PENICILLIUM SIMPLICISSIMUM, NATIVE WITH PEG200 AS CRYOPROTECTANT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 81.188, 81.188, 113.042 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 1.750 |
| R-factor | 0.213 * |
| Rwork | 0.213 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bg4 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 1.720 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.083 * | 0.398 * |
| Number of reflections | 47863 | |
| <I/σ(I)> | 3 | 1 |
| Completeness [%] | 99.8 | 99.4 |
| Redundancy | 5 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8.4 | 4 * | CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.9M (NH4)2SO4, 0.1M TRISHCL PH 8.4 AT 4 C |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 3-6 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) |
