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 2
A stereo figure of the superposition of the region 4 active site of EcDSCD in P3₁21 (sulfate-bound; PDB entry 1c4t) and I4 (PDB entry 6pbr; this work) crystal forms. Chains A, B and C from PDB entry 1c4t are shown in green, cyan and purple, respectively. All of the chains from this work are shown in light grey. Sulfate molecules bind to three residues of the active site: His375, Asp379 and Glu382.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 75| Part 9| September 2019| Pages 616-624

https://doi.org/10.1107/S2053230X19011488

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