1WCQ
Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine.
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 | 2004-09-22 |
| Detector | ADSC CCD |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 143.258, 143.258, 160.250 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 124.030 - 2.100 |
| R-factor | 0.178 |
| Rwork | 0.175 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1euu |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.835 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.830 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.470 |
| Number of reflections | 110911 | |
| <I/σ(I)> | 7.4 | 1.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.2 | 7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 16 % PEG 3350, 0.2 M AMMONIUM CITRATE, pH 5.00 |
