TY - JOUR T1 - Crystallization and preliminary X-ray crystallographic studies on recombinant rat choline acetyltransferase. AU - Lian,Wei, AU - Gu,Yunrong, AU - Pedersen,Brenda, AU - Kukar,Thomas, AU - Govindasamy,Lakshmanan, AU - Agbandje-McKenna,Mavis, AU - Jin,Shouguang, AU - McKenna,Robert, AU - Wu,Donghai, Y1 - 2004/01/23/ PY - 2003/10/14/received PY - 2003/12/08/accepted PY - 2004/1/30/pubmed PY - 2004/10/9/medline PY - 2004/1/30/entrez SP - 374 EP - 5 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 2 N2 - Choline acetyltransferase (ChAT) catalyzes the biosynthesis of the neurotransmitter acetylcholine from acetyl-CoA and choline in cholinergic neurons. Rat ChAT (rChAT) was overexpressed in Escherichia coli, purified by affinity chromatography and crystallized. Diffraction data were collected from a single crystal under cryoconditions at the F1 beamline at the Cornell High Energy Synchrotron Source, with a maximal useful diffraction pattern to 1.55 A resolution. The crystals were shown to belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 138.97, b = 77.67, c = 59.67 A and a scaling R(sym) of 0.054 for 72 446 unique reflections. Packing considerations indicate there to be one molecule per asymmetric unit. It is expected that in the near future the structure of rChAT will be obtained using molecular-replacement methods. Elucidation of the structure of rChAT will aid in the development of therapeutic agents for Alzheimer's disease. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/14747730/Crystallization_and_preliminary_X_ray_crystallographic_studies_on_recombinant_rat_choline_acetyltransferase_ DB - PRIME DP - Unbound Medicine ER -