4V38
Apo-structure of alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-05-09 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 112.220, 57.090, 80.150 |
| Unit cell angles | 90.00, 111.36, 90.00 |
Refinement procedure
| Resolution | 74.650 - 1.960 |
| R-factor | 0.193 |
| Rwork | 0.190 |
| R-free | 0.24413 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4v2u |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.535 |
| 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] | 75.000 | 1.900 |
| High resolution limit [Å] | 1.830 | 1.830 |
| Rmerge | 0.060 | 0.870 |
| Number of reflections | 40997 | |
| <I/σ(I)> | 11.9 | 1.4 |
| Completeness [%] | 98.0 | 87.3 |
| Redundancy | 4.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.2 MG/ML OF PROTEIN 0.1M SUCCINIC ACID, 15% W/V PEG 3350, PH 7.0 |
