8REQ
Crystal structure of reduced ThyX-Y91F mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-03-22 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.978566 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.020, 117.090, 141.967 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.580 - 1.940 |
| R-factor | 0.214 |
| Rwork | 0.213 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.900 |
| Data reduction software | XDS (Jan 10, 2022) |
| Data scaling software | Aimless (0.7.9) |
| Refinement software | BUSTER (2.10.4) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.330 | 90.330 | 1.974 |
| High resolution limit [Å] | 1.940 | 5.266 | 1.940 |
| Rmerge | 0.096 | 0.035 | 2.711 |
| Rmeas | 0.104 | 0.038 | 2.988 |
| Rpim | 0.040 | 0.015 | 1.236 |
| Total number of observations | 460580 | 23110 | 19394 |
| Number of reflections | 68746 | 3701 | 3394 |
| <I/σ(I)> | 9.29 | 33 | 0.56 |
| Completeness [%] | 100.0 | 99.9 | 100 |
| Redundancy | 6.7 | 6.24 | 5.71 |
| CC(1/2) | 0.999 | 0.999 | 0.370 |
| Anomalous redundancy | 3.5 | 3.5 | 3.0 |
| CC(ano) | -0.082 | -0.177 | -0.009 |
| |DANO|/σ(DANO) | 0.7 | 0.7 | 0.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 292 | 1 uL protein at 5-7 mg/ml in Tris 25 mM pH 8 NaCl 150 mM with 1 ul 42-46% w/v PEG 200 in Tris 0.1M pH 7.5 |
