3HFO
Crystal Structure of an Hfq protein from Synechocystis sp.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-06-19 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9000 |
| Spacegroup name | F 2 2 2 |
| Unit cell lengths | 81.470, 86.160, 103.180 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 26.199 - 1.300 |
| R-factor | 0.154 |
| Rwork | 0.152 |
| R-free | 0.20000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hk9 |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.798 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER (2.1.3) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 26.200 | 1.250 | |
| High resolution limit [Å] | 1.210 | 5.430 | 1.210 |
| Rmerge | 0.048 | 0.015 | 0.902 |
| Number of reflections | 52709 | 590 | 3180 |
| <I/σ(I)> | 24.23 | 77.2 | 1.4 |
| Completeness [%] | 96.5 | 87.5 | 79.2 |
| Redundancy | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 292 | 60% Tacsimate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
