1W8N
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-05-06 |
| Detector | RIGAKU-MSC |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.602, 111.608, 143.865 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.710 - 2.100 |
| R-factor | 0.168 |
| Rwork | 0.166 |
| R-free | 0.21900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eut |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.773 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 19.920 |
| High resolution limit [Å] | 2.100 |
| Rmerge | 0.070 |
| Number of reflections | 44697 |
| <I/σ(I)> | 6.9 |
| Completeness [%] | 89.0 |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 16 % PEG 3350, 0.2M AMMONIUM CITRATE. |
