1DVO
THE X-RAY CRYSTAL STRUCTURE OF FINO, A REPRESSOR OF BACTERIAL CONJUGATION
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | BRANDEIS - B1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.570, 38.726, 145.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
Rwork | 0.197 |
R-free | 0.22400 |
RMSD bond length | 0.009 * |
RMSD bond angle | 1.350 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (0.9) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.047 | 0.109 |
Number of reflections | 14726 | |
Completeness [%] | 97.3 | 87 |
Redundancy | 7.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 * | 4 * | drop consists of equal volume of protein and reservoir solutions * |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 * | 4 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | 150 (mM) | ||
3 | 1 | drop | MES | 50 (mM) | |
4 | 1 | drop | beta-mercaptoethanol | 0.1 (%(v/v)) | |
5 | 1 | drop | EDTA | 1 (mM) | |
6 | 1 | reservoir | PEG4000 | 12 (%) | |
7 | 1 | reservoir | Tris-HCl | 50 (mM) |