Increasing the bulk of the 1TEL–target linker and retaining the 10×His tag in a 1TEL–CMG2-vWa construct improves crystal order and diffraction limits

Gajjar, P.L.; Pedroza Romo, M.J.; Litchfield, C.M.; Callahan, M.; Redd, N.; Nawarathnage, S.; Soleimani, S.; Averett, J.; Wilson, E.; Lewis, A.; Stewart, C.; Tseng, Y.-J.; Doukov, T.; Lebedev, A.; Moody, J.D.

doi:10.1107/S2059798323007246

Figure 7
Comparison of the structures analysed in this study. (a) Schematic of the average helical rise of the 1TEL–vWa constructs discussed in this study. The relative rise of a single turn of each helix is denoted by a black arrow. Fused vWa domains are not shown. (b) Plot of the average resolution (orange line) and helical rise (blue line) of the constructs described in this study. (c) The highest resolution structure of the CMG2 vWa domain, PDB entry 1shu (1.5 Å resolution, left), and 1TEL-TV-vWa (1.6 Å resolution, right) are shown in cartoon representation and coloured according to the crystallographic B factor. The B-factor colour scale is given above the images and is the same in the two images. (d) Linker sequences for the constructs used in this study. Residues in the 1TEL C-terminal α-helix are highlighted in cyan, residues in the vWa N-terminal β-sheet are highlighted in magenta and residues that are in neither of these secondary structures are uncoloured. (e) Superposition of batch 1 1TEL-AA-vWa (SUMO) (green), batch 2 1TEL-AA-vWa (SUMO) chain A (yellow) and chain B (brown), 1TEL-TV-vWA (SUMO) (blue), His-1TEL-AA-vWa (wheat) and His-1TEL-TV-vWa (slate) on their 1TEL domains.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 79| Part 10| October 2023| Pages 925-943

https://doi.org/10.1107/S2059798323007246

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