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) |






