6K2H
structural characterization of mutated NreA protein in nitrate binding site from staphylococcus aureus.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-17 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 35.000, 106.302, 33.726 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.800 |
| R-factor | 0.17766 |
| Rwork | 0.175 |
| R-free | 0.22195 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4pau |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.864 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0189) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.096 | 0.455 |
| Number of reflections | 12171 | 150995 |
| <I/σ(I)> | 4.5 | |
| Completeness [%] | 100.0 | |
| Redundancy | 12.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295.15 | HEPES, PEG monomethyl ether 10,000 |
