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Figure 4
Details of the HEX-1 structure. (a) Overall structure of HEX-1 in cartoon representation. (b) Representative region of the electron-density map of HEX-1 obtained by FT-SFX of intracellular crystals at 1.8 Å resolution from a single chip (PDB entry 7asx). The detailed region is marked by a black box in (a). (c) Structural homology of HEX-1 crystallized in insect cells and HEX-1 purified from E. coli and crystallized by sitting-drop vapour diffusion. A backbone representation of the HEX-1 structure (green) obtained from in cellulo diffraction is superimposed with that of the HEX-1 reference structure (PDB code 1khi; blue). The average r.m.s.d. is 0.47 Å for equivalent Cα atoms. The only region showing major structural differences with r.m.s.d.s above 0.6 Å is highlighted by the red box. (d) OMIT map of residues 62–65 of the FT-SFX HEX-1 structure with the same residues in stick representation. The FoFc map (green) of the region of largest r.m.s.d.s with the reference structure, highlighted in (c), is contoured at 3σ.

IUCrJ
Volume 8| Part 4| July 2021| Pages 665-677
ISSN: 2052-2525