6URM

Crystal structure of vaccine-elicited receptor-binding site targeting antibody LPAF-a.01 in complex with Hemagglutinin H1 A/California/04/2009

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	2018-02-10
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.0000
Spacegroup name	P 1 21 1
Unit cell lengths	42.408, 260.836, 66.453
Unit cell angles	90.00, 96.93, 90.00

Refinement procedure

Resolution	40.063 - 2.650
R-factor	0.2172
Rwork	0.215
R-free	0.26190
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5k9o
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.14_3260)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.700
High resolution limit [Å]	2.650	7.190	2.650
Rmerge	0.174	0.076	0.733
Rmeas	0.199	0.088	0.854
Rpim	0.094	0.043	0.428
Number of reflections	37436	1978	1422
<I/σ(I)>	6.7
Completeness [%]	90.8	94.2	71.8
Redundancy	4.1	4.2	3.2
CC(1/2)		0.989	0.561

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	0.2 M (NH4)2SO4 and 23.57% w/v PEG 8000