6VPU
1.90 Angstrom Resolution Crystal Structure Phosphoadenosine Phosphosulfate Reductase (CysH) from Vibrio vulnificus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-10-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 107.758, 76.637, 143.876 |
| Unit cell angles | 90.00, 102.89, 90.00 |
Refinement procedure
| Resolution | 29.800 - 1.900 |
| R-factor | 0.1741 |
| Rwork | 0.172 |
| R-free | 0.20640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sur |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.275 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.744 |
| Rmeas | 0.090 | 0.830 |
| Rpim | 0.039 | 0.362 |
| Number of reflections | 180003 | 8938 |
| <I/σ(I)> | 19.5 | 2.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.1 | 5 |
| CC(1/2) | 0.768 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 292 | Protein: 9.8 mg/ml, 0.5M Sodium chloride, 0.01M Tris pH 8.3, Screen: PEG's II (D10), 0.2 M Sodium acetate, 0.1M Tris pH 8.5, 30% (w/v) PEG 4000 |
