A new crystal form of human acetylcholinesterase for exploratory room-temperature crystallography studies.

ABSTRACT: Structure-guided design of novel pharmacologically active molecules relies at least in part on functionally relevant accuracy of macromolecular structures for template based drug design. Currently, about 95% of all macromolecular X-ray structures available in the PDB (Protein Data Bank) were obtained from diffraction experiments at low, cryogenic temperatures. However, it is known that functionally relevant conformations of both macromolecules and pharmacological ligands can differ at higher, physiological temperatures. We describe in this article development and properties of new human acetylcholinesterase (AChE) crystals of space group P3₁ and a new unit cell, amenable for room-temperature X-ray diffraction studies. We co-crystallized hAChE in P3₁ unit cell with the

SUBMITTER: Gerlits O 

PROVIDER: S-EPMC6679772 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature