3QPG

Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL9-2
Synchrotron site	SSRL
Beamline	BL9-2
Detector technology	CCD
Detector	MARMOSAIC 325 mm CCD
Spacegroup name	C 2 2 21
Unit cell lengths	83.785, 154.834, 77.799
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.500 - 1.790
R-factor	0.149
Rwork	0.148
R-free	0.17900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.518
Data reduction software	DENZO
Data scaling software	SCALA
Phasing software	PHASER (2.1.4)
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall
Low resolution limit [Å]	28.500
High resolution limit [Å]	1.790
Number of reflections	46701
<I/σ(I)>	17.5
Completeness [%]	98.2
Redundancy	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5	293	2 uL of protein solution(15-20 mg/ml, 50 mM TEA, pH 7.5, 100 mM KCL, 2 mM DTT, 10 mM deaza-PLP, 50 mM L-aspartate) mixed with 2 uL reservoir buffer (53-60% saturated ammonium sulfate and 50 mM TEA, pH 7.5), VAPOR DIFFUSION, HANGING DROP, temperature 293K