1CZC

ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-02-15
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 2 2 21
Unit cell lengths	156.350, 85.020, 78.270
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.500
R-factor	0.188
Rwork	0.182
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1yoo
RMSD bond length	0.008
RMSD bond angle	23.700 *
Phasing software	X-PLOR
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	75.000	2.800
High resolution limit [Å]	2.500	2.500
Rmerge	0.054	0.088
Total number of observations	61781 *
Number of reflections	16658
<I/σ(I)>	16.7	64
Completeness [%]	98.8	97.5
Redundancy	3.7	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	20 *	PROTEIN WAS CRYSTALLIZED FROM 1.7M AMMONIUM SULFATE, 0.1 M SODIUM HEPES, 0.167 M GLUTARIC ACID, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	37 (mg/ml)
2	1	drop	sodium succinate	1 (M)	or sodium glutarate
3	1	reservoir	ammonium sulfate	1.7 (M)
4	1	reservoir	HEPES	0.1 (M)