4TMS
PLASTIC ADAPTATION TOWARD MUTATIONS IN PROTEINS: STRUCTURAL COMPARISON OF THYMIDYLATE SYNTHASES
Experimental procedure
Spacegroup name | P 61 2 2 |
Unit cell lengths | 78.300, 78.300, 243.200 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 7.000 - 2.300 * |
R-factor | 0.193 |
RMSD bond length | 0.018 |
RMSD bond angle | 3.600 |
Refinement software | PROLSQ |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 9999.000 * |
High resolution limit [Å] | 2.080 * |
Rmerge | NaN * |
Total number of observations | 66941 * |
Number of reflections | 22275 * |
Completeness [%] | 90.5 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | thymidylate synthases | 2.5 (mg/ml) | |
2 | 1 | drop | EDTA | 1 (mM) | |
3 | 1 | drop | dithiothreitol | 1 (mM) | |
4 | 1 | drop | potassium phosphate | 20 (mM) | |
5 | 1 | drop | ammonium sulfate | 1.15 (M) | |
6 | 1 | reservoir | ammonium sulfate | 2.3 (M) | |
7 | 1 | reservoir | EDTA | 0.2 (mM) | |
8 | 1 | reservoir | dithiothreitol | 1 (mM) | |
9 | 1 | reservoir | potassium phisphate | 20 (mM) |