1QIT

ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191W MUTATION, WITH BOUND MALEATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	297
Detector technology	IMAGE PLATE
Detector	RIGAKU IMAGE PLATE
Spacegroup name	C 2 2 21
Unit cell lengths	157.450, 85.050, 78.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 1.900
R-factor	0.189
Rwork	0.189
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1asa
RMSD bond length	0.020
RMSD bond angle	25.120 *
Data reduction software	R-AXIS
Data scaling software	R-AXIS
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	1.900	1.900
Rmerge	0.042
Number of reflections	38214
Completeness [%]	80.0
Redundancy	1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		PROTEIN SOLUTION: 9MG/ML PROTEIN, 20 MM POTASSIUM PHOSPHATE BUFFER, PH 7.5, 10 UM PLP, 5 MM EDTA, RESERVOIR SOLUTION: 20MM POTASSIUM PHOSPHATE BUFFER, PH 7.5, AND 45-50% AMMONIUM SULFATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	9 (mg/ml)
2	1	drop	potassium phosphate	20 (mM)
3	1	drop	PLP	0.01 (mM)
4	1	drop	EDTA	5 (mM)
5	1	reservoir	ammonium sulfate	40-54 (%)
6	1	reservoir	potassium phosphate	20 (mM)
7	1	drop	inhibitor maleate	5 (mM)