1AAW

THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI

Experimental procedure

Spacegroup name	C 2 2 21
Unit cell lengths	156.800, 86.900, 80.000
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 * - 2.400
R-factor	0.208
RMSD bond length	0.016
RMSD bond angle	6.000
Phasing software	X-PLOR
Refinement software	PROLSQ

Data quality characteristics

	Overall
High resolution limit [Å]	2.400 *
Number of reflections	15069 *
Completeness [%]	72.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *		referred to J.Mol.Biol. 191.301-302 1986 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	drop	sodium phosphate	0.025 (M)
3	1	drop	PLP	0.02 (mM)
4	1	drop	ammonium sulfate	50 (%sat)