1W8O
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-04-12 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.712, 111.168, 142.195 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.710 - 1.700 |
| R-factor | 0.164 |
| Rwork | 0.162 |
| R-free | 0.19700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eut |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.848 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.600 | 1.790 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.070 | 0.320 |
| Number of reflections | 82420 | |
| <I/σ(I)> | 14.8 | 4.4 |
| Completeness [%] | 92.0 | 72 |
| Redundancy | 4 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 16 % PEG 3350, 0.2M AMMONIUM CITRATE |
