4UP3
Crystal structure of the mutant C140S,C286Q thioredoxin reductase from Entamoeba histolytica
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2014-05-04 |
| Detector | MARRESERCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 65.775, 92.048, 102.945 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 68.620 - 1.440 |
| R-factor | 0.12866 |
| Rwork | 0.126 |
| R-free | 0.18073 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4a65 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.032 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0071) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 102.940 | 1.520 |
| High resolution limit [Å] | 1.440 | 1.440 |
| Rmerge | 0.040 | 0.540 |
| Number of reflections | 91837 | |
| <I/σ(I)> | 15 | 1.3 |
| Completeness [%] | 81.2 | 36.4 |
| Redundancy | 3.7 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.9 | 0.2M LITHIUM ACETATE DIHYDRATE, 20% PEG 3350, PH 7.9 |
