Crystallization and Preliminary X-Ray Analysis of Neuropsin, a Serine Protease Expressed in the Limbic System of Mouse Brain |
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Authors: | Tadaaki Kishi Masato Kato Toshiyuki Shimizu Keiko Kato Kazumasa Matsumoto Shigetaka Yoshida Sadao Shiosaka Toshio Hakoshima |
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Institution: | aDepartment of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara, 630-01, Japan;bDepartment of Cell Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara, 630-01, Japan;cDepartment of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara, 630-01, Japan |
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Abstract: | Neuropsin (Mr25 032) is a serine protease expressed in the limbic system of mouse brain. It has been implicated in various neurological processes including formation of memory and may be important as a drug target in the treatment of epilepsy. The recombinant protein was produced using a baculovirus expression system and was purified. Two crystal forms were obtained by a hanging-drop vapor-diffusion method with polyethylene glycol. Preliminary X-ray crystallographic analysis revealed that crystal form I belongs to triclinic space groupP1 with unit cell dimensionsa= 97.16 Å,b= 97.12 Å,c= 46.75 Å and α = 99.17°, β = 99.77°, γ = 117.35°. Self-rotation function analysis of these data of form I indicates the position of a noncrystallographic threefold axis. There are six molecules in the crystallographic asymmetric unit. Crystal form II also belongs to triclinic space groupP1 but has unit cell dimensions ofa= 38.40 Å,b= 55.16 Å,c= 65.37 Å and α = 95.38°, β = 89.98°, γ = 110.46° with two molecules in the crystallographic asymmetric unit. Form II has a noncrystallographic twofold axis. Intensity data to 3.1 Å resolution for form I and to 2.2 Å resolution for form II have been collected. |
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