3DIN
Crystal structure of the protein-translocation complex formed by the SecY channel and the SecA ATPase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-15 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97950 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 101.616, 156.003, 358.155 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 - 4.500 |
| R-factor | 0.279 |
| Rwork | 0.279 |
| R-free | 0.30300 |
| Structure solution method | SAD, MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tf2 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 4.770 |
| High resolution limit [Å] | 4.500 | 4.500 |
| Number of reflections | 34733 | |
| <I/σ(I)> | 16.1 | 2 |
| Completeness [%] | 97.7 | 89.7 |
| Redundancy | 11.6 | 8.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 298 | 20% PEG 3350, 200mM (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, temperature 298K | |
| 1 | 7.5 | 298 | 20% PEG 3350, 200mM (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, temperature 298K | |
| 1 | 7.5 | 298 | 20% PEG 3350, 200mM (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, temperature 298K | |
| 1 | 7.5 | 298 | 20% PEG 3350, 200mM (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, temperature 298K |






