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. |