1ZEA
Structure of the anti-cholera toxin antibody Fab fragment TE33 in complex with a D-peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-10-26 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8095 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 100.638, 108.862, 40.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.000 - 1.780 |
| R-factor | 0.201 |
| Rwork | 0.198 |
| R-free | 0.24800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tet |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.912 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.1) |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.000 | 1.810 |
| High resolution limit [Å] | 1.780 | 1.780 |
| Number of reflections | 40461 | |
| <I/σ(I)> | 14.14 | 3.27 |
| Completeness [%] | 93.4 | 89.4 |
| Redundancy | 4.78 | 3.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 293 | PEG 8000, citrat buffer, potassium chloride, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
