1AKC

Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking its pyridoxal-5'-phosphate-binding lysine residue

Experimental procedure

Spacegroup name	C 2 2 21
Unit cell lengths	69.800, 91.300, 127.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.300
R-factor	0.172
RMSD bond length	0.011
RMSD bond angle	0.042
Refinement software	PROLSQ

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	2.300 *
Rmerge	0.075 *
Total number of observations	38502 *
Number of reflections	16434 *
Completeness [%]	88.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	other *	7.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
2	1	drop	PEG	9-14 (%)
3	1	drop	sodium phosphate	20 (mM)
4	1	drop		0.9 (M)
5	1	drop	PPxy-Glu	20 (mM)
6	1	drop	apoenzyme	10 (mg/ml)
7	1	reservoir	PEG	18-28 (%)
8	1	reservoir	sodium phosphate	20 (mM)