5G26

Unveiling the Mechanism Behind the in-meso Crystallization of Membrane Proteins

Summary for 5G26

• Entry DOI: 10.2210/pdb5g26/pdb
• Descriptor: INTIMIN, (2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate, (2R)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate, ... (4 entities in total)
• Functional Keywords: membrane protein, lyotropic liquid crystalline systems, in meso crystallisation
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 29100.54

Authors

Zabara, A.,Newman, J.,Peat, T.S. (deposition date: 2016-04-07, release date: 2017-02-15, Last modification date: 2024-01-10)

Primary citation

Zabara, A.,Meikle, T.G.,Newman, J.,Peat, T.S.,Conn, C.E.,Drummond, C.J.
The Nanoscience Behind the Art of in-Meso Crystallization of Membrane Proteins.
Nanoscale, 9:754-, 2017

PubMed Abstract: The structural changes occurring at the nanoscale level within the lipid bilayer and driving the in-meso formation of large well-diffracting membrane protein crystals have been uniquely characterized for a model membrane protein, intimin. Importantly, the order to order transitions taking place within the bilayer and the lipidic nanostructures required for crystal growth have been shown to be general, occurring for both the cubic and the sponge mesophase crystallization pathways. For the first time, a transient fluid lamellar phase has been observed and unambiguously assigned for both crystallization pathways, present at the earliest stages of protein crystallogenesis but no longer observed once the crystals surpass the size of the average lyotropic liquid crystalline domain. The reported time-resolved structural investigation provides a significantly improved and general understanding of the nanostructural changes taking place within the mesophase during in-meso crystallization which is a fundamental advance in the enabling area of membrane protein structural biology.

PubMed: 27976759
DOI: 10.1039/C6NR07634C

Experimental method

X-RAY DIFFRACTION (2.42 Å)