1GXQ
Crystal structure of the PhoB effector domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 110 |
Collection date | 2000-12-15 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 84.650, 37.290, 30.510 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.000 - 2.000 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.26600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qqi |
RMSD bond length | 0.007 |
RMSD bond angle | 1.285 * |
Data reduction software | MOSFLM |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.200 | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.072 | 0.206 |
Total number of observations | 62124 * | |
Number of reflections | 6550 | |
<I/σ(I)> | 6.3 | 3.1 |
Completeness [%] | 94.4 | 71.1 |
Redundancy | 9.5 | 6.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6.5 | pH 6.50 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | bis-Tris | 10 (mM) | |
2 | 1 | drop | 0.5 (M) | ||
3 | 1 | drop | protein | 11 (mg/ml) | |
4 | 1 | reservoir | sodium cacodylate | 100 (mM) | pH6.5 |
5 | 1 | reservoir | sodium acetate | 200 (mM) | |
6 | 1 | reservoir | PEG8000 | 30 (%(w/v)) |