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516 Halorhodopsin: light-driven ion pumping made simple? Lars-Oliver Essen Halorhodopsin, a light-driven halide pump, is the second archaeal H. salinarum [11,12,13?]. Tetragonal 2D crystals formed rhodopsin involved in ion pumping to be studied at high resolution spontaneously in vivo when halorhodopsin was homo- by X-ray crystallography. Like its cousin bacteriorhodopsin, logously overproduced in the recombinant H. salinarum halorhodopsin couples vectorial ion transport to the isomerisation strain D2. Unlike the naturally occurring 2D crystals of state of a covalently linked retinal. Given the similarity and bacteriorhodopsin, which constitute the so-called purple interconvertability of these two ion pumps, a unified mechanism for membrane, the alternating inside-out and outside-in ion translocation by archaeal rhodopsins is now emerging. arrangement of halorhodopsin tetramers suggested that these 2D crystals were physiologically irrelevant artefacts Addresses of the overexpression conditions. Nevertheless, low-resolution Department of Chemistry, Philipps University, Hans-Meerwein-Strasse, data of up to 5 ? resolution proved the bacteriorhodopsin- D-35032 Marburg, Germany; e-mail: essen@chemie.uni-marburg.de like architecture of halorhodopsin. Current Opinion in Structural Biology 2002, 12:516–522 0959-440X/02/$ — see front matter The 1.8 ? X-ray structure of H. salinarum halorhodopsin ? 2002 Elsevier Science Ltd. All rights reserved. [10??] was the second structure of a membrane protein to be crystallised in a lipidic cubic phase [14,15?]. In these 3D Introduction crystals, halorhodopsin assembled into trimers and the Two functions can be