5UTX
Crystal structure of thioredoxin-disulfide reductase from Vibrio vulnificus CMCP6 - apo form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-11-30 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 120.031, 120.031, 79.185 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 47.830 - 2.460 |
| R-factor | 0.2023 |
| Rwork | 0.200 |
| R-free | 0.25380 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cl0 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.478 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | HKL-3000 |
| Refinement software | PHENIX (dev_2614) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.490 |
| High resolution limit [Å] | 2.450 | 6.650 | 2.450 |
| Rmerge | 0.065 | 0.040 | 0.960 |
| Rmeas | 0.071 | 0.044 | 1.052 |
| Rpim | 0.027 | 0.017 | 0.419 |
| Total number of observations | 160021 | ||
| Number of reflections | 24257 | ||
| <I/σ(I)> | 9.7 | ||
| Completeness [%] | 98.7 | 99.2 | 75.7 |
| Redundancy | 6.6 | 6.1 | 5.8 |
| CC(1/2) | 0.997 | 0.698 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 289 | 20% PEG1000, 100 mM potassium/sodium phosphate, 200 mM sodium chloride |
