7OH8
R17A mutant of Hfq protein from Neisseria meningitidis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-10-19 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 61.683, 106.252, 27.904 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.860 - 1.700 |
| R-factor | 0.2432 |
| Rwork | 0.240 |
| R-free | 0.29530 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4pn0 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.475 |
| Data reduction software | XDS (20210323) |
| Data scaling software | Aimless (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.250 | 40.250 | 1.730 |
| High resolution limit [Å] | 1.700 | 9.000 | 1.700 |
| Rmerge | 0.245 | 0.048 | 2.040 |
| Rmeas | 0.255 | 0.051 | 2.128 |
| Rpim | 0.071 | 0.015 | 0.596 |
| Total number of observations | 268092 | 1886 | 13244 |
| Number of reflections | 21006 | 186 | 1077 |
| <I/σ(I)> | 9.4 | 32 | 1.4 |
| Completeness [%] | 99.8 | 99.2 | 96.1 |
| Redundancy | 12.8 | 10.1 | 12.3 |
| CC(1/2) | 0.997 | 0.999 | 0.566 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 293 | PEG 1500, SPG pH 4 |
