1AKA

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING ITS PYRIDOXAL-5'-PHOSPHATE-BINDING LYSINE RESIDUE

Experimental procedure

Spacegroup name	P 1
Unit cell lengths	55.870, 58.800, 75.810
Unit cell angles	85.26, 108.96, 115.57

Refinement procedure

Resolution	10.000 - 2.100
R-factor	0.169
RMSD bond length	0.010
RMSD bond angle	1.410 *
Refinement software	PROLSQ

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	2.100 *
Rmerge	0.053 *
Total number of observations	56002 *
Number of reflections	41517 *
Completeness [%]	81.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG4000	8.5-9.5 (%)
2	1	drop	sodium phosphate	20 (mM)	pH7.5
3	1	drop	enzyme	12 (mg/ml)
4	1	reservoir	PEG4000	17-19 (%)