1ACM
ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY
Experimental procedure
Spacegroup name | P 3 2 1 |
Unit cell lengths | 122.200, 122.200, 156.200 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 8.000 - 2.800 |
R-factor | 0.18 * |
Rwork | 0.180 |
RMSD bond length | 0.012 |
RMSD bond angle | 3.100 |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.800 * |
Number of reflections | 33351 * |
Redundancy | 6.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Microdialysis * | 5.9 * | 21 * | Krause, K.L., (1987) J.Mol.Biol., 193, 527. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | buttom | enzyme | 15-16 (mg/ml) | |
2 | 1 | reservior | maleic acid | 50 (mM) | |
3 | 1 | reservoir | N-(phosphonacetyl)-L-aspartate | 1 (mM) | |
4 | 1 | reservoir | 3 (mM) | ||
5 | 1 | reservoir | N-ethylmorpholine |