2TCL
STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR
Experimental procedure
| Spacegroup name | I 4 | 
| Unit cell lengths | 86.960, 86.960, 40.960 | 
| Unit cell angles | 90.00, 90.00, 90.00 | 
Refinement procedure
| Resolution | 6.000  * - 2.200 | 
| R-factor | 0.21  *  | 
| Rwork | 0.162 | 
| RMSD bond length | 0.013  *  | 
| RMSD bond angle | 3.000  *  | 
| Phasing software | X-PLOR | 
| Refinement software | X-PLOR | 
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 20.000 *  | 
| High resolution limit [Å] | 2.200 *  | 
| Rmerge | 0.065 *  | 
| Total number of observations | 18085 *  | 
| Number of reflections | 7339 *  | 
| Completeness [%] | 92.0 *  | 
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details | 
| 1 | 1 | drop | protein | 13 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 2 (mM) | ||
| 4 | 1 | reservoir | PEG4000 | 25 (%) | |
| 5 | 1 | reservoir | sodium cacodylate | 0.1 (M) | |
| 6 | 1 | reservoir | ammonium acetate | 0.2 (M) | 






