1RJ9
Structure of the heterodimer of the conserved GTPase domains of the Signal Recognition Particle (Ffh) and Its Receptor (FtsY)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 75.040, 83.680, 94.020 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.900 |
R-factor | 0.239 |
Rwork | 0.206 |
R-free | 0.23900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | the structures of isolated FtsY and Ffh NG domain |
RMSD bond length | 0.005 |
RMSD bond angle | 1.400 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.077 | 0.767 * |
Total number of observations | 305159 * | |
Number of reflections | 47344 * | |
<I/σ(I)> | 16.9 | 3.1 |
Completeness [%] | 99.3 * | 97.9 * |
Redundancy | 6.3 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.5 * | 4 * | PEG 8000, Hepes, NaCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 10 (%) | |
2 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |