Microscopy Techniques Sees Individual Atoms For First Time

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Cryo-electron microscopy breaks a key barrier that will allow the working of proteins to be probed in unprecedented detail. By achieving Atomic resolution using Cryogenic-electron microscopy (cryo-EM) the working of Proteins that cannot be easily examined by other imaging techniques e.g. X Ray crystallography, be understood. The number of protein structures being determined by Cryo- electron microscopy is growing at an explosive rate. 

Cryo-EM is a decades old technique that determines the shape of flash-frozen samples by firing electrons at them and recording the resulting images. Advances in technology for detecting the ricocheting electrons and in image-analysis software catalysed a 'resolution revolution' that started around 2013. This led to protein structures that were sharper than ever before - and nearly as good as those obtained from X Rav crystallography, an older technique that infers structures from diffraction patterns made by protein crystals when they are bombarded with X Rays.

Atomic-resolution maps are precise enough to unambiguously discern the position of individual atoms in a protein, at a resolution of around 1.2 angstroms. These structures are especially useful for understanding how enzymes work and using those insights to identify drugs that can block their activity. To push atomic resolution, working on an iron storing protein called Apoferritin was done. Because of its rock-like stability, the protein has become a test bed for Cryo-EM: a structure of the protein with a resolution of 1.54 angstroms was the previous record. 

Cryo-EM is suited to large, stable molecules that can withstand electron bombardment without jiggling around - so molecular machines, often built from dozens of proteins, are good targets. None has proved more suitable than ribosomes, which are braced by rigid twists of RNA. The solution of ribosome structures by XRay crystallography won three chemists the 2009 Nobel prize in chemistry- but those efforts took decades. 


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