3K38
Crystal Structure of B/Perth Neuraminidase D197E mutant
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 | 2008-05-22 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.95364 |
| Spacegroup name | P 1 |
| Unit cell lengths | 111.155, 123.683, 123.789 |
| Unit cell angles | 90.04, 90.19, 90.19 |
Refinement procedure
| Resolution | 61.780 - 2.190 |
| R-factor | 0.19247 |
| Rwork | 0.191 |
| R-free | 0.21989 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3k36 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.506 |
| 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] | 61.780 | 2.320 |
| High resolution limit [Å] | 2.190 | 2.200 |
| Rmerge | 0.102 | 0.365 |
| Number of reflections | 316772 | |
| <I/σ(I)> | 8.1 | 2.6 |
| Completeness [%] | 94.6 | 92.7 |
| Redundancy | 2 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 281.15 | 12-17% w/v PEG 3350, 0.2-0.3M Na2 SO4, 5mM YCl3, VAPOR DIFFUSION, SITTING DROP, temperature 281.15K, PH7 |
