1M6N
Crystal structure of the SecA translocation ATPase from Bacillus subtilis
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Temperature [K] | 100 |
Detector technology | AREA DETECTOR |
Collection date | 1997-12-15 |
Detector | MARRESEARCH |
Wavelength(s) | 0.986 |
Spacegroup name | P 31 1 2 |
Unit cell lengths | 130.833, 130.833, 150.350 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.240 - 2.700 |
R-factor | 0.22 |
Rwork | 0.220 |
R-free | 0.30400 * |
Structure solution method | MIR |
RMSD bond length | 0.013 |
RMSD bond angle | 1.740 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | DM |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 * | 2.750 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.078 * | |
Number of reflections | 40372 | |
<I/σ(I)> | 18.9 | 2.14 |
Completeness [%] | 99.6 * | 0.973 |
Redundancy | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 299 | Weinkauf, S., (2001) Acta Crystallogr., Sect.D, 57, 559. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15-20 (mg/ml) | |
2 | 1 | drop | ammonium sulfate | 300 (mM) | |
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | drop | BES | 20 (mM) | pH7.0 |
5 | 1 | reservoir | ammonium sulfate | 46-52 (%sat) | |
6 | 1 | reservoir | glycerol | 28-32 (%(v/v)) | |
7 | 1 | reservoir | BES | 20-100 (mM) | pH7.0 |