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Monomer/Oligomer Quasi-Racemic Protein Crystallography
journal contribution
posted on 2016-10-21, 19:33 authored by Shuai Gao, Man Pan, Yong Zheng, Yichao Huang, Qingyun Zheng, Demeng Sun, Lining Lu, Xiaodan Tan, Xianglong Tan, Huan Lan, Jiaxing Wang, Tian Wang, Jiawei Wang, Lei LiuRacemic or quasi-racemic
crystallography recently emerges as a
useful technology for solution of the crystal structures of biomacromolecules.
It remains unclear to what extent the biomacromolecules of opposite
handedness can differ from each other in racemic or quasi-racemic
crystallography. Here we report a finding that monomeric d-ubiquitin (Ub) has propensity to cocrystallize with different dimers,
trimers, and even a tetramer of l-Ub. In these cocrystals
the unconnected monomeric d-Ubs can self-assemble to form
pseudomirror images of different oligomers of l-Ub. This
monomer/oligomer cocrystallization phenomenon expands the concept
of racemic crystallography. Using the monomer/oligomer cocrystallization
technology we obtained, for the first time the X-ray structures of
linear M1-linked tri- and tetra-Ubs and a K11/K63-branched tri-Ub.