8T2C
Crystal structure of O-acetyl-L-serine sulfhydrylase A (CysK) from Staphylococcus aureus NCTC 8325 complexed with a CymR pentapeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-01-30 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 50.608, 94.515, 56.078 |
| Unit cell angles | 90.00, 108.50, 90.00 |
Refinement procedure
| Resolution | 43.070 - 1.800 |
| R-factor | 0.2237 |
| Rwork | 0.223 |
| R-free | 0.24550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.574 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.260 | 1.840 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.094 | 1.724 |
| Rmeas | 0.102 | 1.856 |
| Rpim | 0.039 | 0.683 |
| Total number of observations | 319273 | 19493 |
| Number of reflections | 46258 | 2716 |
| <I/σ(I)> | 9.8 | 1.1 |
| Completeness [%] | 99.8 | |
| Redundancy | 6.9 | 7.2 |
| CC(1/2) | 0.998 | 0.618 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 0.2 M ammonium acetate, 0.1M HEPES pH 7.5, 23-25% PEG3350 |
