1FIP
THE STRUCTURE OF FIS MUTANT PRO61ALA ILLUSTRATES THAT THE KINK WITHIN THE LONG ALPHA-HELIX IS NOT DUE TO THE PRESENCE OF THE PROLINE RESIDUE
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 79.080, 51.120, 47.290 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.900 |
| R-factor | 0.199 |
| Rwork | 0.199 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 3.221 * |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.900 * |
| Rmerge | 0.042 * |
| Total number of observations | 47664 * |
| Number of reflections | 14082 * |
| Completeness [%] | 92.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8.2 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | drop | 0.5 (M) | ||
| 3 | 1 | drop | Tris-HCl | 10 (mM) | |
| 4 | 1 | drop | 1 (M) | ||
| 5 | 1 | reservoir | 2.0 (M) |
