Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization

Mitropoulou, A.N.; Ceska, T.; Heads, J.T.; Beavil, A.J.; Henry, A.J.; McDonnell, J.M.; Sutton, B.J.; Davies, A.M.

doi:10.1107/S2053230X20001466

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Structure FabXol1¹ of the omalizumab-derived Leu158Pro mutant (FabXol1). (a) The FabXol1¹ structure contains two molecules (pink and yellow/green and gray) in the asymmetric unit. (b) Interface between residues 155–159 of the Cκ domain (blue) of molecule FabXol1^1A and the V_H domain of a symmetry-related molecule (gray). An ethylene glycol molecule (EG) is also bound at this interface. (c) Interface between the Cκ domain (gray) of molecule FabXol1^1B and the Cκ domain (yellow) and Cγ1 domain (pink) of the noncrystallographic symmetry-related molecule, FabXol1^1A. (d) Conformations for the CDRH1–3 residues, and their crystal packing interactions with the V_L domain (and Cκ domain in the Fabs), are similar for FabXol¹ (pink), FabXol1^1A (yellow), FabXol1^1B (blue) and scFvXol (gray).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 76| Part 3| March 2020| Pages 116-129

https://doi.org/10.1107/S2053230X20001466

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