8E9K

Crystal structure of wild-type E. coli aspartate aminotransferase bound to maleate at 278 K

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.3.1
Synchrotron site	ALS
Beamline	8.3.1
Temperature [K]	278
Detector technology	PIXEL
Collection date	2021-06-01
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	0.9795
Spacegroup name	P 63
Unit cell lengths	143.830, 143.830, 81.570
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.080 - 1.830
R-factor	0.1559
Rwork	0.153
R-free	0.18320
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1x28
RMSD bond length	0.005
RMSD bond angle	0.812
Data reduction software	xia2
Data scaling software	DIALS
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	62.160	1.860
High resolution limit [Å]	1.830	1.830
Rmerge	0.200	1.800
Number of reflections	84225	4169
<I/σ(I)>	6.5
Completeness [%]	100.0
Redundancy	10.5
CC(1/2)	0.996	0.348

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	HEPES, ammonium sulfate, maleate, PEG 400