TY - JOUR
T1 - Crystallization and preliminary X-ray analysis of neuropsin, a serine protease expressed in the limbic system of mouse brain
AU - Kishi, Tadaaki
AU - Kato, Masato
AU - Shimizu, Toshiyuki
AU - Kato, Keiko
AU - Matsumoto, Kazumasa
AU - Yoshida, Shigetaka
AU - Shiosaka, Sadao
AU - Hakoshima, Toshio
N1 - Funding Information:
We thank M. Suzuki and Y. Fujii for their help in data collection at the Photon Factory, High Energy Physics Laboratory, Japan. This work was supported by Grants in Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan. M.K. was supported by a research fellowship from the Japan Society for the Promotion of Science.
PY - 1997/4
Y1 - 1997/4
N2 - Neuropsin (M(r) 25 032) 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 group P1 with unit cell dimensions a = 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 group P1 but has unit cell dimensions of a = 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 resolution for form II have been collected.
AB - Neuropsin (M(r) 25 032) 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 group P1 with unit cell dimensions a = 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 group P1 but has unit cell dimensions of a = 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 resolution for form II have been collected.
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U2 - 10.1006/jsbi.1997.3862
DO - 10.1006/jsbi.1997.3862
M3 - Article
C2 - 9169235
AN - SCOPUS:0030898658
SN - 1047-8477
VL - 118
SP - 248
EP - 251
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 3
ER -