3FIS
THE MOLECULAR STRUCTURE OF WILD-TYPE AND A MUTANT FIS PROTEIN: RELATIONSHIP BETWEEN MUTATIONAL CHANGES AND RECOMBINATIONAL ENHANCER FUNCTION OR DNA BINDING
Experimental procedure
Spacegroup name | P 21 21 21 |
Unit cell lengths | 79.400, 50.900, 47.100 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 * - 2.300 |
R-factor | 0.183 |
Rwork | 0.183 |
RMSD bond length | 0.017 * |
RMSD bond angle | 3.600 * |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.250 * |
Rmerge | 0.032 * |
Total number of observations | 30267 * |
Number of reflections | 6451 * |
Completeness [%] | 68.0 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 18 (mg/ml) | |
2 | 1 | drop | 1 (M) | ||
3 | 1 | drop | Tris-HCl | 20 (mM) | |
4 | 1 | drop | 2-mercaptoethanol | 50 (mM) | |
5 | 1 | reservoir | ammonium phosphate | 1.3 (M) | can be replaced with PEG400 |