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 |