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. 2019 Feb 15;10:763. doi: 10.1038/s41467-019-08738-5

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Crystal structures of closed prefusion structure of B41 SOSIP.664 Env trimer. a, b Views of the Fab complex down the trimer axis with gp120 in pink and gp41 in cyan. The cartoon representation is overlaid with a transparent molecular surface. Fabs PGT124 (dark gray) and 35O22 (green) are from the 3.50 and 3.80 Å structures in space groups P23 (a) and P6₃ (b), respectively. c Comparison of the protomer/trimer backbones from crystal structures of trimers of clade A (BG505 SOSIP.664, bound and unbound), B (JRFL SOSIP.664), G (X1193.c1 SOSIP.664), and the new B41 SOSIP.664 structure at 3.50 Å. d Glycosylation observed in the electron density maps in the two different B41 SOSIP.664 crystal structures. The blue, gray, and green bars along the Y-axis represent the number of N-glycan moieties of N-acetylglucosamine (NAG/GlcNAc) (maximum possible, two), β-d-mannopyranose (BMA) (maximum, one), and α-d-mannopyranose (MAN) (maximum, eight), respectively. The X-axis represents N-glycosylation sites on B41 SOSIP.664. e, f Side views of B41 SOSIP.664 protomer (gp120: light blue, gp41: light orange) in cartoon representation, overlaid with a transparent molecular surface showing two conformational states of the free N-terminus FP (pink) going away from (3.50 Å) and towards (3.80 Å) the C-terminus (i.e. proximal to the membrane)