T.R.Huber
et al.
(2018).
Installing Guest Molecules at Specific Sites within Scaffold Protein Crystals.
Bioconjug Chem,
29,
17-22.
PubMed id: 29232505
DOI: 10.1021/acs.bioconjchem.7b00668
Installing Guest Molecules at Specific Sites within Scaffold Protein Crystals.
T.R.Huber,
E.C.McPherson,
C.E.Keating,
C.D.Snow.
ABSTRACT
Protein crystals are porous self-assembling materials that can be rapidly
evolved by mutagenesis. We aimed to develop scaffold assisted crystallography
techniques in an engineered protein crystal with large pores (>13 nm). Guest
molecules were installed via a single covalent bond to attempt to reduce the
conformational freedom and achieve high-occupancy structures. We used four
different conjugation strategies to attach guest molecules to three different
cysteine sites within pre-existing protein crystals. In all but one case, the
presence of the adduct was obvious in the electron density. Structure
determination of larger guest molecules may be feasible due to the large pores
of the engineered scaffold crystals.