The first electron crystallographic protein structure to achieve atomic resolution was bacteriorhodopsin, determined by Richard Henderson and coworkers at the Medical Research Council Laboratory of Molecular Biology in 1990. However, already in 1975 Unwin and Henderson had determined the first membrane protein structure at intermediate resolution (7 Ångström), showing for the first time the internal structure of a membrane protein, with its alpha-helices standing perpendicular to the plane of the membrane. Since then, several other high-resolution structures have been determined by electron crystallography, including the light-harvesting complex, the nicotinic acetylcholine receptor, and the bacterial flagellum. The highest resolution protein structure solved by electron crystallography of 2D crystals is that of the water channel aquaporin-0. In 2012, Jan Pieter Abrahams and coworkers extended electron crystallography to 3D protein nanocrystals by rotation electron diffraction (RED).