4V3B
The structure of alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis in complex with the donor product CMP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-03-10 |
| Detector | DECTRIS PIXEL |
| Spacegroup name | P 65 |
| Unit cell lengths | 113.555, 113.555, 65.740 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.180 |
| R-factor | 0.18906 |
| Rwork | 0.186 |
| R-free | 0.23794 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4v2u |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.679 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.260 |
| High resolution limit [Å] | 2.180 | 2.180 |
| Rmerge | 0.090 | 0.890 |
| Number of reflections | 25784 | |
| <I/σ(I)> | 9.5 | 1.2 |
| Completeness [%] | 99.3 | 97.7 |
| Redundancy | 3.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.2 MG/ML PROTEIN CONCENTRATION 0.2 M AMMONIUM CHLORIDE, 20% W/V PEG 3350 |
