9MEH

Crystal structure of the dimodular LgrA after protein ligation

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	200
Detector technology	PIXEL
Collection date	2020-12-09
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.98
Spacegroup name	P 21 21 21
Unit cell lengths	119.235, 166.281, 178.491
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.380 - 3.600
R-factor	0.2672
Rwork	0.267
R-free	0.27340
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.446
Data reduction software	HKL-2000 (721)
Data scaling software	HKL-2000 (721)
Phasing software	PHASER (2.9.0)
Refinement software	PHENIX (1.21.1_5286)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.660
High resolution limit [Å]	3.600	3.600
Rmerge	0.129	2.490
Rmeas	0.135	2.604
Rpim	0.039	0.751
Number of reflections	41605	2030
<I/σ(I)>	18.6	0.875
Completeness [%]	99.9	100
Redundancy	11.6	11.3
CC(1/2)	1.000	0.489

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.8	277.15	2% PEG 2000 MME, 0.9 M sodium succinate, 0.1 M HEPES pH 6.8, 0.1 M ammonium succinate, 0.5 mM 1-nonanoyl-2-hydroxy-sn-glycero-3-phosphocholine (09:0 lyso-PC)