3EEB
Structure of the V. cholerae RTX cysteine protease domain
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 | 2008-01-30 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 44.491, 66.099, 136.051 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.100 |
R-factor | 0.2015 |
Rwork | 0.199 |
R-free | 0.24279 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.333 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.180 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.117 | 0.530 |
Number of reflections | 23713 | |
<I/σ(I)> | 3.2 | |
Completeness [%] | 96.3 | 97.4 |
Redundancy | 6.3 | 5.5 |
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 |