5ERW

Structure of HCV E2 glycoprotein antigenic Epitope II bound to the broadly neutralizing antibody HC84-26

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	Cu FINE FOCUS
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2014-12-05
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 2 21 21
Unit cell lengths	37.700, 101.240, 180.320
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.080 - 2.900
R-factor	0.2195
Rwork	0.215
R-free	0.25800
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.016
RMSD bond angle	1.487
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.22)
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	45.080	51.684	3.060
High resolution limit [Å]	2.900	9.170	2.900
Rmerge		0.041	0.454
Rmeas	0.097
Rpim	0.048	0.028	0.277
Total number of observations	58541	2165	7157
Number of reflections	15740
<I/σ(I)>	11.3	21.8	2.8
Completeness [%]	98.2	99.3	95.4
Redundancy	3.7	3.6	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH	5.5	293	15% (w/v) PEG 10,000, 0.1 M Sodium citrate/ Citric acid pH 5.5, 2% (v/v) Dioxane