@misc{10481/74151,
year = {2022},
month = {1},
url = {http://hdl.handle.net/10481/74151},
abstract = {Protein crystallization is an astounding feat of nature. Even
though proteins are large, anisotropic molecules with complex,
heterogeneous surfaces, they can spontaneously group into twoand
three-dimensional arrays with high precision. And yet,
the biggest hurdle in this assembly process, the formation of a
nucleus, is still poorly understood. In recent years, the two-step
nucleation model has emerged as the consensus on the subject,
but it still awaits extensive experimental verification. Here, we set
out to reconstruct the nucleation pathway of the candidate protein
glucose isomerase (GI), for which there have been indications
that it may follow a two-step nucleation pathway under certain
conditions. We find that the precursor phase present during the
early stages of the reaction process is nanoscopic crystallites that
have lattice symmetry equivalent to the mature crystals found at
the end of a crystallization experiment. Our observations underscore
the need for experimental data at a lattice-resolving resolution
on other proteins so that a general picture of protein crystal
nucleation can be formed.},
organization = {FWO	G0H5316N	
1516215N},
organization = {French Infrastructure for Integrated Structural Biology (FRISBI)	ANR-10-INBS-0005-02},
organization = {Grenoble Alliance for Integrated Structural and Cell Biology (GRAL)within the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) Chemistry, Biology, and Health, European Graduate School (CBHEUR-GS)	ANR-17-EURE-0003},
publisher = {National Academy of Sciences},
keywords = {Nucleation},
keywords = {Proteins},
keywords = {Self-assembly},
keywords = {Crystallization},
keywords = {Precursor phase},
title = {Nucleation of glucose isomerase protein crystals in a nonclassical disguise: The role of crystalline precursors},
doi = {10.1073/pnas.2108674119},
author = {Van Driessche, Alexander Edgard Suzanne},
}