1HK9
Crystal structure of the Hfq protein from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 5.2R |
| Synchrotron site | ELETTRA |
| Beamline | 5.2R |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2002-07-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 |
| Unit cell lengths | 61.350, 61.350, 166.100 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.150 |
| R-factor | 0.208 |
| Rwork | 0.208 |
| R-free | 0.26200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kq1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.610 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 2.210 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.098 | 0.270 |
| Total number of observations | 139736 * | |
| Number of reflections | 19131 * | |
| <I/σ(I)> | 12.9 | 4.5 |
| Completeness [%] | 99.8 * | 96.5 |
| Redundancy | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 4.6 | 20 * | CRYSTALS WERE OBTAINED BY VAPOR DIFFUSION IN 2UL SITTING DROPS. THE RESERVOIR CONTAINED 25% PEG 4000, 0.2 M NH4-ACETATE AND 0.2 M NA-ACETATE PH 4.6. CRYSTALLIZATION WERE CARRIED OUT AT 20C. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 25 (%) | |
| 3 | 1 | reservoir | ammonium acetate | 0.2 (M) | |
| 4 | 1 | reservoir | sodium acetate | 0.2 (M) | pH4.6 |
