Crystal structures of the selenoprotein glutathione peroxidase 4 in its apo form and in complex with the covalently bound inhibitor ML162

Moosmayer, D.; Hilpmann, A.; Hoffmann, J.; Schnirch, L.; Zimmermann, K.; Badock, V.; Furst, L.; Eaton, J.K.; Viswanathan, V.S.; Schreiber, S.L.; Gradl, S.; Hillig, R.C.

doi:10.1107/S2059798320016125

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Crystals obtained for different variants of selenocysteine-containing human GPX4. (a) GPX4^WT. The largest rods are about 200 × 40 × 40 µm in size. (b) GPX4^WT modified with ML162 (racemate). The crystal indicated by the red arrow is about 50 × 10 × 10 µm in size. (c) GPX4^C66S modified with enantiopure (S)-ML162 (the largest rod is about 200 × 30 × 30 µm in size).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 77| Part 2| February 2021| Pages 237-248

https://doi.org/10.1107/S2059798320016125

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