5VRG

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2016-08-03
Detector	MARRESEARCH
Wavelength(s)	0.9792
Spacegroup name	P 21 21 21
Unit cell lengths	87.764, 158.026, 44.763
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.068 - 2.518
R-factor	0.2147
Rwork	0.212
R-free	0.27100
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.029
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (dev_2747)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	43.068	158.026	2.526
High resolution limit [Å]	2.518	11.686	2.518
Rmeas	0.221	0.075	0.965
Rpim	0.081	0.030	0.352
Number of reflections	21672
<I/σ(I)>	9.8
Completeness [%]	98.9	97.5	98
Redundancy	7.3	5.7	7.5
CC(1/2)	0.994	0.999	0.764

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	LIPIDIC CUBIC PHASE	6.5	293	50 mM ADA pH 6.5 24% PEG 400