3QN6

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	84.749, 154.678, 79.147
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	35.229 - 1.790
R-factor	0.1533
Rwork	0.151
R-free	0.18800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.017
RMSD bond angle	1.486
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.15)
Phasing software	MOLREP
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	39.574	39.574	1.840
High resolution limit [Å]	1.790	8.010	1.790
Rmerge		0.024	0.428
Total number of observations		1410	11977
Number of reflections	48807
<I/σ(I)>	10.7	26.4	1.7
Completeness [%]	99.1	79.7	99.7
Redundancy	3.4	2.9	3.3

Crystallization Conditions

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