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