3K39
Crystal Structure of B/Perth Neuraminidase D197E mutant in complex with Peramivir
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-17 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.95665 |
| Spacegroup name | P 1 |
| Unit cell lengths | 111.964, 124.874, 125.245 |
| Unit cell angles | 90.03, 92.11, 91.27 |
Refinement procedure
| Resolution | 55.900 - 2.540 |
| R-factor | 0.19884 |
| Rwork | 0.198 |
| R-free | 0.21388 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3k38 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.569 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.580 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.209 | 0.557 |
| Number of reflections | 286795 | |
| <I/σ(I)> | 4.7 | 2 |
| Completeness [%] | 95.2 | 90.3 |
| Redundancy | 3.4 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 281.15 | 12-17% w/v PEG 3350, 0.2-0.3M Na2 SO4, 5mM YCl3, VAPOR DIFFUSION, HANGING DROP, temperature 281.15K, PH7 |
