4DVC
Structural and functional studies of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera toxin production
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-07-09 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9536 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 62.654, 89.520, 64.263 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.132 - 1.200 |
R-factor | 0.1198 |
Rwork | 0.119 |
R-free | 0.13920 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.205 |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (dev_1031) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.200 | |
High resolution limit [Å] | 1.200 | 1.200 |
Rmerge | 0.103 | 0.103 |
Number of reflections | 56644 | |
<I/σ(I)> | 18 | 3.1 |
Completeness [%] | 99.7 | 97.4 |
Redundancy | 14 | 12.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | hanging drop | 6.4 | 277.15 | PEG 4000, MES, pH 6.4, hanging drop, temperature 277.15K |