Table 2 cryo-EM data collection, map, and model refinement statistics

	(DH270.4-CH848.10.17)	(DH270.5-CH848.10.17)	(DH270.6-CH848.10.17)	(VRC01-CH848.0526.25)	(VRC01-CH848.10.17)	(DH270.6-CH848.0526.25)	(VRC01-CH848.0836.10)	(VRC01-CH848.0358.80)
Data Collection
Microscope	FEI Titan Krios
Detector	Gatan K3
Magnification	105000
Voltage (kV)	300
Electron dose (e^-/Å²)	60	60	53.15	69.98	60	60	60	60
Pixel Size (Å)	1.066	1.066	1.066	1.066	1.066	1.066	1.066	1.066
Defocus Range (µm)	~0.8–4.3	~0.7–4.1	~0.5–4.1	~0.5–3.1	~0.5–3.5	~0.5–3.5	~0.5–3.5	~0.5–3.5
Reconstruction Software cryoSPARC
Symmetry	C3	C3	C3	C3	C3	C3	C3	C3
Particles	107890	76211	106823	252873	35839	119542	28746	46336
Box size (pix)	384	384	384	384	384	384	384	384
Resolution (Å) (FSC0.143)^a	3.3	4.0	3.82	4.0	4.5	3.9	4.6	4.9
Coordinate Refinement (Phenix)^b
Protein residues	2490	2496	2490	2514	2457	2574	2505	2523
R.m.s. deviations
Bond lengths (Å)	0.006	0.008	0.006	0.004	0.005	0.006	0.004	0.006
Bond angles (°)	0.915	1.100	1.055	0.845	0.894	1.041	0.949	0.997
Validation
Molprobity score	1.57	1.71	1.71	1.53	1.80	1.76	1.71	1.90
Clash score	3.13	4.02	4.37	2.96	5.01	4.26	4.65	6.60
Favored rotamers (%)	99.72	99.68	99.30	99.77	99.81	99.73	99.59	100
EMRinger Score	1.95	0.36	1.74	1.66	1.65	1.49	1.31	0.56
Ramachandran plot
Favored regions (%)	92.46	90.94	91.93	93.14	90.56	89.78	92.51	90.15
Disallowed regions (%)	0.32	0.44	0.41	0.24	0.41	0.35	0.12	0.24

^a Resolutions are reported according to the FSC 0.143 gold-standard criterion.
^b Statistics are reported for the protein residues within the complex excluding the antibody constant domains.

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