Open AccessNucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors
Author(s) -
Alexander E. S. Van Driessche,
Wai Li Ling,
Guy Schoehn,
Mike Sleutel
Publication year - 2022
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2108674119
Subject(s) - nucleation , crystallization , protein crystallization , nucleus , crystallite , lattice (music) , isomerase , chemical physics , crystallography , anisotropy , chemistry , crystal (programming language) , biophysics , materials science , physics , biology , computer science , biochemistry , microbiology and biotechnology , enzyme , programming language , organic chemistry , quantum mechanics , acoustics
Significance The ability of proteins to self-assemble into complex, hierarchical structures has been the inspiration for the bottom-up design of a class of biomaterials with proteins as their building blocks. The earliest stages of formation often involve the passing of an activation barrier under the form of nucleus formation, a quaternary protein complex that templates incoming molecules to proper registry. For protein crystallization, the consensus has emerged that the fastest route toward a nucleus follows a winding path: first, densification, followed by symmetry formation. In this contribution, we show that this need not be the case for the protein glucose isomerase, which seems to follow the simplest path to a nucleus, making crystalline clusters from the earliest detectable beginnings.