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 5
Crystallization and structural details of His-1TEL-AA-vWa. (a) Representative crystals of His-1TEL-AA-vWa. The scale bar is 100 µm. (b) Representative diffraction pattern from a His-1TEL-AA-vWa crystal. (c) Unit-cell packing of a His-1TEL-AA-vWa crystal with the 1TEL domain in magenta and the vWa domain in wheat. The unit cell is indicated by a thin black line. (d) Detail of the interaction between a vWa domain (wheat) and its host 1TEL domain (magenta). The protein is shown in cartoon representation with selected side chains shown as sticks and transparent spheres. (e) As in (d) but showing the interaction between the vWa domain (salmon) and a vWa domain (wheat) from an adjacent TELSAM polymer. (f) As in (d) and (e) but highlighting the contacts made by a vWa domain to a second vWa domain and its host 1TEL domain. (g) As in (d) but highlighting the position of the iodinated tyrosine residues (small green spheres) relative to the 1TEL–vWa polymer. (h) As in (d) but highlighting (magenta spheres) the N-terminal 10×His tag of the 1TEL domain. The structure of chain A of the 1TEL-TV-vWA (SUMO) structure is superimposed via its 1TEL domain and shown in cyan (1TEL) and yellow (vWa).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798323007246

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