A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat

Geerds, C.; Bleymüller, W.M.; Meyer, T.; Widmann, C.; Niemann, H.H.

doi:10.1107/S2059798322000432

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Crystal packing. (a) View along the a axis of InlB₃₉₂_T332E crystal form I. The b axis and part of the c axis (54.59 and 226.72 Å) are shown horizontally and vertically, respectively. There is one molecule per asymmetric unit. (b) View along the a axis of InlB₃₉₂_wt. The b axis and part of the c axis (148.41 and 220.02 Å) are shown horizontally and vertically, respectively. There are three molecules per asymmetric unit related by translational noncrystallographic symmetry. The translational component along b is close to 1/3. Chains A, B and C are shown in dark blue, blue and cyan, respectively.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 3| March 2022| Pages 310-320

https://doi.org/10.1107/S2059798322000432

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