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) |