4ASL
Structure of Epa1A in complex with the T-antigen (Gal-b1-3- GalNAc)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-03-06 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 74.600, 103.900, 69.400 |
| Unit cell angles | 89.90, 90.00, 89.90 |
Refinement procedure
| Resolution | 10.000 - 1.240 |
| R-factor | 0.11864 |
| Rwork | 0.117 |
| R-free | 0.15521 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | EPA1A WILD TYPE COMPLEXED WITH LACTOSE CONTAMINANT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.524 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | REFMAC |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 1.310 |
| High resolution limit [Å] | 1.240 | 1.240 |
| Rmerge | 0.030 | 0.550 |
| Number of reflections | 75251 | |
| <I/σ(I)> | 22.7 | 2.7 |
| Completeness [%] | 98.7 | 97.5 |
| Redundancy | 4.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 0.1M MES PH6.5 0.2M AMMOMIUM SULFATE 25% PEG 5000 MME 0.025 M LACTOSE |
