1MZ6
Trypanosoma rangeli sialidase in complex with the inhibitor DANA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE D41A |
| Synchrotron site | LURE |
| Beamline | D41A |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-11-27 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.375 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.200, 93.800, 105.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 * - 2.900 |
| R-factor | 0.20884 |
| Rwork | 0.205 |
| R-free | 0.31400 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Unliganded T. rangeli sialidase 1MZ5 |
| RMSD bond length | 0.019 * |
| RMSD bond angle | 0.063 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.980 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.138 * | 0.306 * |
| Total number of observations | 112960 * | |
| Number of reflections | 17063 | |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 18 * | PEG-8000, ammonium sulfate, morpholinoethanesulfonate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 7 (mg/ml) | |
| 2 | 1 | reservoir | PEG8000 | 17 (%) | |
| 3 | 1 | reservoir | ammonium sulfate | 100 (mM) | |
| 4 | 1 | reservoir | MOPS | 50 (mM) | pH6.5 |
