5WT5
L-homocysteine-bound NifS from Helicobacter pylori
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2016-04-20 |
| Detector | RAYONIX MX225HE |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 102.440, 102.320, 132.050 |
| Unit cell angles | 90.00, 90.10, 90.00 |
Refinement procedure
| Resolution | 47.782 - 1.900 |
| R-factor | 0.1847 |
| Rwork | 0.184 |
| R-free | 0.20890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ecx |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.775 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.11.1_2575: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.782 | 1.968 |
| High resolution limit [Å] | 1.897 | 1.900 |
| Rmerge | 0.075 | 0.791 |
| Rpim | 0.046 | 0.473 |
| Number of reflections | 221285 | |
| <I/σ(I)> | 11.91 | 1.7 |
| Completeness [%] | 99.9 | 99.76 |
| Redundancy | 3.7 | 3.7 |
| CC(1/2) | 0.996 | 0.529 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | HEPES/NaOH, PEG 4000, glycerol, isopropanol, L-homocysteine |
