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![[Figure 3]](ba5149fig3mag.jpg)
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Figure 3
Temperature-controlled kinetic crystallography to study the structural details of substrate and product traffic in the enzyme acetylcholinesterase (adapted from Bourgeois & Weik, 2009  ). (a) Soaking AChE crystals at room temperature in an excess of the substrate acetylthiocholine led to (b) a steady-state population trapped at 100 K, in which a substrate, a choline and an acetyl group were located in the active-site gorge (Colletier et al., 2006). (c) Using UV irradiation of caged choline as a reaction trigger during a brief excursion to room temperature (d) an intermediate state was trapped in which a small movement of Trp84 opened a channel from the active site to the solvent region (Colletier et al., 2007). (e) When several consecutive data sets were collected at 150 K from crystals of acetylcholinesterase in complex with a nonhydrolysable substrate analogue (Colletier et al., 2008), a similar movement of Trp84 (f) as seen in (d) was observed. |
![[Figure 3]](ba5149fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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