5M33
Structural tuning of CD81LEL (space group P21)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-11-23 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.972499 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 31.445, 75.846, 37.363 |
| Unit cell angles | 90.00, 107.12, 90.00 |
Refinement procedure
| Resolution | 25.997 - 1.280 |
| R-factor | 0.1382 |
| Rwork | 0.136 |
| R-free | 0.17290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1g8q |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.180 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 26.000 | 1.300 |
| High resolution limit [Å] | 1.280 | 1.280 |
| Rmerge | 0.062 | 0.380 |
| Number of reflections | 38224 | |
| <I/σ(I)> | 21.6 | 3.4 |
| Completeness [%] | 88.6 | 40.9 |
| Redundancy | 5.2 | 3.8 |
| CC(1/2) | 0.934 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 294.15 | Protein: 10 mg/ml Buffer: 0.1 M MIB pH 5.0, 25% w/v PEG 1500 grown in presence of synthetic claudin-I long-extracellular-loop (CLDN1-EL1) - but not visible in electron density. cryo-protectant: 25% glycerol + peptide |
