3GCD
Structure of the V. cholerae RTX cysteine protease domain in complex with an aza-Leucine peptide inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 140 |
| Detector technology | CCD |
| Collection date | 2008-03-06 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.560, 65.854, 254.880 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.350 |
| R-factor | 0.22064 |
| Rwork | 0.218 |
| R-free | 0.26499 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ID 3EEB |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.303 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.430 |
| High resolution limit [Å] | 2.350 | 2.350 |
| Rmerge | 0.099 | 0.454 |
| Number of reflections | 31246 | |
| <I/σ(I)> | 13.6 | 2.3 |
| Completeness [%] | 89.0 | 61.4 |
| Redundancy | 4.4 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | 30%PEG3350, 15% MPD, 0.1M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
