3ITF
Structural basis for the inhibitory function of the CPXP adaptor protein
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-29 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9184, 0.9798, 0.9799 |
| Spacegroup name | P 65 |
| Unit cell lengths | 61.463, 61.463, 130.082 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 53.220 - 1.450 |
| R-factor | 0.169 |
| Rwork | 0.168 |
| R-free | 0.18900 |
| Structure solution method | MAD |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.416 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELXCD |
| Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.220 | 1.500 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Number of reflections | 49268 | |
| <I/σ(I)> | 18.9 | 2.4 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.7 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | 18% PEG 3350, 0.1M Sodium chloride, 0.01M Tris-HCl, 5% Glycerol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
