9EEJ

Crystal structure of E. coli aspartate transcarbamoylase in the R-state complexed with CP, succinate, ATP, and Mg2+

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-03-27
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9795
Spacegroup name	P 21 21 21
Unit cell lengths	129.049, 148.793, 207.866
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	103.900 - 3.000
R-factor	0.2185
Rwork	0.218
R-free	0.24880
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.518
Data reduction software	DIALS (3.18.0)
Data scaling software	DIALS (3.18.0)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.21.1_5286)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	103.900	3.110
High resolution limit [Å]	3.000	3.000
Rmerge	0.268	1.027
Rpim	0.121	0.454
Number of reflections	80502	7971
<I/σ(I)>	4.2	0.7
Completeness [%]	99.3
Redundancy	5.8
CC(1/2)	0.966	0.642

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	295	Protein solution: 0.016 mM ATCase in 40 mM Tris pH 7.0, 20 mM CP, 20 mM succinate, 30 mM MgCl2, and 10 mM ATP Well solution: 0.1 M Bis-Tris pH 6.5 and 20-25% PEG 300 Drops: 0.001 mL each of protein and well solution