1BNC
THREE-DIMENSIONAL STRUCTURE OF THE BIOTIN CARBOXYLASE SUBUNIT OF ACETYL-COA CARBOXYLASE
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.900, 96.100, 180.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.183 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.300 |
| Refinement software | TNT |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 100.000 * |
| High resolution limit [Å] | 2.200 * |
| Rmerge | 0.039 * |
| Total number of observations | 93923 * |
| Number of reflections | 41566 * |
| Completeness [%] | 75.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microdialysis * | 7 * | 4 * | Waldrop, G., (1994) J. Mol. Biol, 235, 367. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 2 | potassium phosphate | 10 (mM) | |
| 2 | 1 | 2 | EDTA | 1 (mM) | |
| 3 | 1 | 2 | DTT | 2 (mM) | |
| 4 | 1 | 2 | 1 (mM) | ||
| 5 | 1 | 1 | protein | 10 (mg/ml) |






