Installing Guest Molecules at Specific Sites within
Scaffold Protein Crystals
Thaddaus
R. Huber
Eli C. McPherson
Carolyn E. Keating
Christopher D. Snow
10.1021/acs.bioconjchem.7b00668.s001
https://acs.figshare.com/articles/journal_contribution/Installing_Guest_Molecules_at_Specific_Sites_within_Scaffold_Protein_Crystals/5725831
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.
2017-12-12 00:00:00
Guest
pore
protein
scaffold
guest molecules
Scaffold Protein Crystals Protein crystals