1BG4
XYLANASE FROM PENICILLIUM SIMPLICISSIMUM
Experimental procedure
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 5.2R |
Synchrotron site | ELETTRA |
Beamline | 5.2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE AREA DETECTOR |
Collection date | 1997-07 |
Detector | MARRESEARCH |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 81.020, 81.020, 113.400 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 1.750 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.22900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1xyz |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 | 1.790 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.059 * | 0.232 * |
Number of reflections | 43712 | |
<I/σ(I)> | 15 | 4 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.4 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 1.9M (NH4)2SO4, 0.1M TRISHCL PH 8.4 AT 4 C, temperature 277K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.9 (M) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
3 | 1 | drop | pyrazole | 3-6 (mg/ml) |