1CVF
STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.700, 41.700, 73.000 |
| Unit cell angles | 90.00, 104.60, 90.00 |
Refinement procedure
| Resolution | 7.000 - 2.250 |
| R-factor | 0.176 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.040 |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.250 * |
| Rmerge | 0.081 * |
| Total number of observations | 15073 * |
| Number of reflections | 8124 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 4 * | Alexander, R.S., (1991) Biochemistry, 30, 11064. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 0.3 (mM) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | drop | 150 (mM) | ||
| 4 | 1 | drop | 3 (mM) | ||
| 5 | 1 | reservoir | ammonium sulfate | 1.75-2.5 (M) |
