1MAT
STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME
Experimental procedure
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.000, 61.700, 54.500 |
| Unit cell angles | 90.00, 107.30, 90.00 |
Refinement procedure
| Resolution | 52.000 * - 2.500* |
| R-factor | 0.182 |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.900 |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.500 * |
| Rmerge | 0.035 * |
| Number of reflections | 8054 * |
| Completeness [%] | 93.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.8 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 42 (mg/ml) | |
| 2 | 1 | drop | sodium cacodylate | 25 (M) | |
| 3 | 1 | drop | 25 (mM) | ||
| 4 | 1 | drop | 100 (mM) | ||
| 5 | 1 | drop | 1 (mM) | ||
| 6 | 1 | drop | PEG4000 | 14 (%(w/v)) | |
| 7 | 1 | drop | octyl beta-glucoside | 0.5 (%(w/v)) | |
| 8 | 1 | reservoir | PEG4000 | 23-35 (%) |






