3FZY
Crystal Structure of Pre-cleavage Form of Cysteine Protease Domain from Vibrio cholerae RtxA Toxin
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 | 2008-09-11 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.055, 66.373, 137.958 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 23.670 - 1.950 |
| R-factor | 0.1713 |
| Rwork | 0.169 |
| R-free | 0.21616 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3eeb |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.696 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0051) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 1.980 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.076 | 0.448 |
| Number of reflections | 32396 | |
| <I/σ(I)> | 3.1 | |
| Completeness [%] | 99.4 | 95.3 |
| Redundancy | 6.7 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | The PEGs II Suite, condition 72 mixed 1:1 v/v with 7.3mg/mL protein, 0.3M NaCl, 0.5mM InsP6, 10mM Tris-HCl (pH 7.4), VAPOR DIFFUSION, SITTING DROP, temperature 295K, pH 8.5 |
