title: In-situ and real-time growth observation of high-quality protein crystals under quasi-microgravity on earth.
abstract: Precise protein structure determination provides significant information on life science research, although high-quality crystals are not easily obtained. We developed a system for producing high-quality protein crystals with high throughput. Using this system, gravity-controlled crystallization are made possible by a magnetic microgravity environment. In addition, in-situ and real-time observation and time-lapse imaging of crystal growth are feasible for over 200 solution samples independently. In this paper, we also report results of crystallization experiments for two protein samples. Crystals grown in the system exhibited magnetic orientation and showed higher and more homogeneous quality compared with the control crystals. The structural analysis reveals that making use of the magnetic microgravity during the crystallization process helps us to build a well-refined protein structure model, which has no significant structural differences with a control structure. Therefore, the system contributes to improvement in efficiency of structural analysis for "difficult" proteins, such as membrane proteins and supermolecular complexes.
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Akira
authors.initials: A
authors.lastname: Nakamura
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Jun
authors.initials: J
authors.lastname: Ohtsuka
authors.affiliation: Institute for Innovation, Ajinomoto Co. Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki, Kanagawa 210-8681, Japan.
authors.forename: Tatsuki
authors.initials: T
authors.lastname: Kashiwagi
authors.affiliation: Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan.
authors.forename: Nobutaka
authors.initials: N
authors.lastname: Numoto
authors.affiliation: National Institute for Materials Science, 3-13 Sakura, Tsukuba, Ibaraki 305-0003, Japan.
authors.forename: Noriyuki
authors.initials: N
authors.lastname: Hirota
authors.affiliation: Kiyohara Optics Inc., 6-23-2 Shinjuku, Shinjuku-ku, Tokyo 160-0022, Japan.
authors.forename: Takahiro
authors.initials: T
authors.lastname: Ode
authors.affiliation: National Institute for Materials Science, 3-13 Sakura, Tsukuba, Ibaraki 305-0003, Japan.
authors.forename: Hidehiko
authors.initials: H
authors.lastname: Okada
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Koji
authors.initials: K
authors.lastname: Nagata
authors.affiliation: Kiyohara Optics Inc., 6-23-2 Shinjuku, Shinjuku-ku, Tokyo 160-0022, Japan.
authors.forename: Motosuke
authors.initials: M
authors.lastname: Kiyohara
authors.affiliation: Institute for Innovation, Ajinomoto Co. Inc., 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki, Kanagawa 210-8681, Japan.
authors.forename: Ei-Ichiro
authors.initials: E
authors.lastname: Suzuki
authors.affiliation: Research Reactor Institute, Kyoto University, Kumatori, Sennan, Osaka 590-0494, Japan.
authors.forename: Akiko
authors.initials: A
authors.lastname: Kita
authors.affiliation: National Institute for Materials Science, 3-13 Sakura, Tsukuba, Ibaraki 305-0003, Japan.
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Wada
authors.affiliation: Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
authors.forename: Masaru
authors.initials: M
authors.lastname: Tanokura
mesh_terms: D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D018534:Earth, Planet; D005118:Extraterrestrial Environment; D008280:Magnetics / Q000379:methods*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D059008:Time-Lapse Imaging; D014893:Weightlessness
chemical_list: D011506:Proteins