3JV2
Crystal Structure of B. subtilis SecA with bound peptide
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 | 2007-04-11 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.97950 |
Spacegroup name | P 41 |
Unit cell lengths | 106.724, 106.724, 175.605 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.500 |
Rwork | 0.208 |
R-free | 0.25800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tf5 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 67929 | |
<I/σ(I)> | 26.4 | 2.8 |
Completeness [%] | 98.3 | 100 |
Redundancy | 5.4 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 298 | 0.1M sodium citrate, 8% PEG 4000, 0.1M NaCl, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |