Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant

Andi, B.; Soares, A.S.; Shi, W.; Fuchs, M.R.; McSweeney, S.; Liu, Q.

doi:10.1107/S2053230X19011488

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
Molecular packing of EcDSCD in three different crystal forms. (a) In space group P3₁21 (PDB entry 1c4t), the trimer (in red) cannot form the 24-mer biological assembly. The dimensions of the unit cell (blue lines) shown in the plane are a = b = 112.18 Å. (b) In space group F432 (PDB entry 1scz), the packing forms a 24-mer biological assembly (in red). The dimensions of the unit cell (blue lines) shown in the plane are a = b = 220.58 Å. (c) In space group I4 (PDB entry 6pbr, this work), the packing shows a 24-mer biological assembly (in red). The dimensions of the unit cell (red lines) shown in the plane are a = b = 128.60 Å. The building block for all of the crystal forms of EcDSCD is a trimer [shown in red in the P3₁21 (d), F432 (e) and I4 (f) crystal forms]. Intermolecular interactions between the trimers are unique in the different crystal forms, as shown, while the monomer/trimer itself shows a minimal conformational change between crystal forms [Figs. 3