1CHM
ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE AS DEDUCED FROM CRYSTAL STRUCTURES
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 60.830, 110.550, 62.630 |
| Unit cell angles | 90.00, 102.22, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 * |
| Rwork | 0.177 |
| RMSD bond length | 0.010 * |
| RMSD bond angle | 1.900 * |
| Refinement software | EREF |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.000 * | |
| High resolution limit [Å] | 2.370 * | 2.370 * |
| Rmerge | 0.039 * | |
| Total number of observations | 79941 * | |
| Number of reflections | 26026 * | |
| Completeness [%] | 41.5 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | protein | 30 (mg/ml) | |
| 2 | 1 | 1 | PEG6000 | 20 (%(w/v)) | |
| 3 | 1 | 1 | sodium phosphate | 0.2 (M) | |
| 4 | 1 | 1 | inhibitor | 0.01 (M) |






