4CMS
X-RAY ANALYSES OF ASPARTIC PROTEINASES IV. STRUCTURE AND REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN
Experimental procedure
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 79.980, 114.120, 72.760 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.200 |
| R-factor | 0.158 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.032 |
| Refinement software | RESTRAIN |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.200 * |
| Rmerge | 0.089 * |
| Number of reflections | 16823 * |
| Completeness [%] | 96.6 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 10 (mg/ml) | |
| 2 | 1 | 1 | 50 (mM) | ||
| 3 | 1 | 2 | 1 (M) | ||
| 4 | 1 | 2 | 0.1 (M) |






