2FSF
Escherichia coli SecA, the preprotein translocase dimeric ATPase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9393 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.030, 90.171, 163.049 |
| Unit cell angles | 90.00, 100.48, 90.00 |
Refinement procedure
| Resolution | 19.980 - 2.000 |
| Rwork | 0.213 |
| R-free | 0.26100 |
| Structure solution method | MAD |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.210 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHELXD |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.100 | |
| High resolution limit [Å] | 2.000 | 6.000 | 2.000 |
| Rmerge | 0.042 | 0.034 | 0.352 |
| Number of reflections | 140049 | 4162 | 16916 |
| <I/σ(I)> | 12.49 | 32.1 | 2.3 |
| Completeness [%] | 97.1 | 97 | 86.7 |
| Redundancy | 3.2 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | ||||
| 1 | ||||
| 1 |
