5MH4
Crystal Structure of Lactococcus lactis Thioredoxin Reductase (FR conformation)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-1 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-03-16 |
| Detector | DECTRIS PILATUS3 2M |
| Wavelength(s) | 0.96501 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 120.540, 120.540, 60.470 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.370 - 2.140 |
| R-factor | 0.1796 |
| Rwork | 0.177 |
| R-free | 0.23730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f6m |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.985 |
| Data reduction software | XDS (November 3, 2014) |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (6.3) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 85.240 | 2.220 |
| High resolution limit [Å] | 2.140 | 2.140 |
| Rmerge | 0.127 | 1.744 |
| Number of reflections | 25158 | |
| <I/σ(I)> | 12.3 | 1.3 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 8.38 | 8.46 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 292 | 35% PEG 1500, 400 mM Li2SO4, 20 mM HEPES |
