2A5D
Structural basis for the activation of cholera toxin by human ARF6-GTP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0781 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 44.915, 91.446, 98.547 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.740 - 1.800 |
| R-factor | 0.16855 |
| Rwork | 0.167 |
| R-free | 0.19939 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1. mouse ARF1 (1O3Y) 2. CTA1 (1S5E) |
| RMSD bond length | 0.017 |
| RMSD bond angle | 2.025 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 36064 | |
| Completeness [%] | 93.3 | 56.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | PEG2000mme, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
