Significance What are the odds that a 1,000 Å 3 -sized metal-binding site will find its cargo parsing a volume of 30 trillion Å 3 by a random 3D diffusional process? Establishing a unique paradigm in the field of copper biology, we show that cells use a stunningly simple method to beat these odds by reducing the dimensionality of the problem through exploitation of cellular membranes as scaffolding components. We demonstrate that the copper delivery chaperone for the essential enzyme Cu/Zn superoxide dismutase 1 (SOD1) has the ability to bind to bilayers and that this previously unknown membrane binding interface is important for copper distribution to SOD1.

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Since its debut in the mid 70ties, electron crystallography has been a valuable alternative in the structure determination of biological macromolecules. Its reliance on single- or double-layered two-dimensionally ordered arrays and the ability to obtain structural information from small and disordered crystals make this approach particularly useful for the study of membrane proteins in a lipid bilayer environment. Despite its unique advantages, technological hurdles have kept electron crystallography from reaching its full potential. Addressing the issues, recent initiatives developed high-throughput pipelines for crystallization and screening. Adding progress in automating data collection, image analysis and phase extension methods, electron crystallography is poised to raise its profile and may lead the way in exploring the structural biology of macromolecular complexes.