Monomer/Oligomer
Quasi-Racemic Protein Crystallography
Version 2 2016-10-28, 16:34
Version 1 2016-10-21, 19:33
Posted on 2016-10-21 - 00:00
Racemic 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.
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Gao, Shuai; Pan, Man; Zheng, Yong; Huang, Yichao; Zheng, Qingyun; Sun, Demeng; et al. (2016). Monomer/Oligomer
Quasi-Racemic Protein Crystallography. ACS Publications. Collection. https://doi.org/10.1021/jacs.6b09545
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AUTHORS (14)
SG
Shuai Gao
MP
Man Pan
YZ
Yong Zheng
YH
Yichao Huang
QZ
Qingyun Zheng
DS
Demeng Sun
LL
Lining Lu
XT
Xiaodan Tan
XT
Xianglong Tan
HL
Huan Lan
JW
Jiaxing Wang
TW
Tian Wang
JW
Jiawei Wang
LL
Lei Liu