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Acetylcholinesterase (AChE) is one of nature's fastest enzymes, despite the fact that its three-dimensional structure reveals its active site to be deeply sequestered within the molecule. This raises questions with respect to traffic of substrate to, and products from, the active site, which may be investigated by time-resolved crystallography. In order to address one aspect of the feasibility of performing time-resolved studies on AChE, a data set has been collected using the Laue technique on a trigonal crystal of Torpedo californica AChE soaked with the reversible inhibitor edrophonium, using a total X-ray exposure time of 24 ms. Electron-density maps obtained from the Laue data, which are of surprisingly good quality compared with similar maps from monochromatic data, show essentially the same features. They clearly reveal the bound ligand, as well as a structural change in the conformation of the active-site Ser200 induced upon binding.


R B Ravelli, M L Raves, Z Ren, D Bourgeois, M Roth, J Kroon, I Silman, J L Sussman. Static Laue diffraction studies on acetylcholinesterase. Acta crystallographica. Section D, Biological crystallography. 1998 Nov 1;54(Pt 6 Pt 2):1359-66

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PMID: 10089512

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