1AIA

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

Experimental procedure

Spacegroup name	P 1 21 1
Unit cell lengths	86.900, 79.800, 89.900
Unit cell angles	90.00, 118.90, 90.00

Refinement procedure

Resolution	10.000 - 2.200
R-factor	0.21
Rwork	0.210
RMSD bond length	0.014
RMSD bond angle	3.020
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000 *
High resolution limit [Å]	2.200 *
Rmerge	0.061 *
Number of reflections	49125 *
Completeness [%]	90.1 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15.1 (mg/mL)
2	1	drop	maleate	100 (mM)
3	1	drop	sodium chloride	0.45-0.55 (M)
4	1	drop	PEG	16 (%(w/v))
5	1	drop	sodium phosphate	20 (mM)
6	1	reservoir	PEG	32 (%(w/v))
7	1	reservoir	sodium chloride	0.9-1.1 (M)
8	1	reservoir	sodium phosphate	20 (mM)