3AAT

ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE

Experimental procedure

Spacegroup name	C 2 2 21
Unit cell lengths	156.000, 87.600, 78.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.500 *
R-factor	0.215
RMSD bond length	0.011
RMSD bond angle	0.073
Refinement software	PROLSQ

Data quality characteristics

	Overall
High resolution limit [Å]	2.500 *
Rmerge	0.067 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	50 (%sat)
2	1	reservoir	potassium phosphate	20 (mM)