1SLL
SIALIDASE L FROM LEECH MACROBDELLA DECORA
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-12-24 |
Detector | MACSCIENCE |
Spacegroup name | P 1 |
Unit cell lengths | 46.364, 69.275, 72.469 |
Unit cell angles | 113.48, 95.41, 107.31 |
Refinement procedure
Resolution | 6.000 - 2.000 |
R-factor | 0.166 * |
Rwork | 0.167 |
R-free | 0.22600 * |
Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.640 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | X-PLOR (3.85) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.090 |
High resolution limit [Å] | 2.000 | 2.020 |
Rmerge | 0.044 * | 0.088 |
Total number of observations | 145108 * | |
Number of reflections | 48481 * | |
<I/σ(I)> | 16 | 13.5 |
Completeness [%] | 96.5 | 94.2 |
Redundancy | 3 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.3 | THE PROTEIN WAS CRYSTALLIZED BY MACROSEEDING IN 20% PEG 6000, 0.25 M NACL, 0.1 M CACODYLATE BUFFER, PH 6.3., macroseeding |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 5 (mg/ml) | |
2 | 1 | reservoir | cacodylate | 0.1 (M) | |
3 | 1 | reservoir | PEG6000 | 20 (%) | |
4 | 1 | reservoir | 0.25 (M) |