1N1T
Trypanosoma rangeli sialidase in complex with DANA at 1.6 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-01-31 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 73.945, 96.258, 106.513 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 * - 1.600 |
| R-factor | 0.17424 |
| Rwork | 0.173 |
| R-free | 0.19700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n1s |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.610 |
| 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] | 30.000 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.066 * | 0.192 * |
| Total number of observations | 351240 * | |
| Number of reflections | 95328 | |
| Completeness [%] | 94.6 | 94.4 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | PEG-8000, sodium cacodylate, ammonium sulfate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 20 (mM) | |
| 3 | 1 | drop | sodium acetate | 30 (mM) | pH7.0 |
| 4 | 1 | reservoir | PEG8000 | 16 (%(w/w)) | |
| 5 | 1 | reservoir | sodium cacodylate | 50 (mM) | |
| 6 | 1 | reservoir | ammonium sulfate | 100 (mM) | pH6.5 |
