5I82
First Crystal Structure of E.coli Based Recombinant Diphtheria Toxin Mutant CRM197
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-13 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 69.214, 69.167, 127.882 |
| Unit cell angles | 90.09, 90.01, 82.02 |
Refinement procedure
| Resolution | 29.080 - 2.350 |
| R-factor | 0.20958 |
| Rwork | 0.207 |
| R-free | 0.25026 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ae1 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.174 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.390 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.051 | 0.424 |
| Number of reflections | 98137 | |
| <I/σ(I)> | 18.2 | 2.3 |
| Completeness [%] | 98.4 | 97.7 |
| Redundancy | 2.6 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 292 | Protein: 22.9 mg/ml, 0.15M Sodium chloride,0.01M Tris-HCL (pH 8.3); Screen: Classics II (G2), 0.2M Lithium sulfate, 0.1M Bis-Tris (pH 5.5), 25% (w/v) PEG 3350 |
