Crystallization and Structure Analysis of Lectins from Various Sources
| Project/Area Number |
02680047
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
結晶学
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| Research Institution | Osaka University |
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Principal Investigator |
MATSUURA Yoshiki Institute for Protein research Osaka University Associate Profesor, たんぱく質研究所, 助教授 (90029968)
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| Co-Investigator(Kenkyū-buntansha) |
KATSUBE Yukiteru 大阪大学, たんぱく質研究所, 教授 (20032013)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1991: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1990: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Protein Crystallization / Lectin / X-ray Structure Analysis / Flammulina veltipes / beta-varrel Structure / Immunoglobulin Fold / Molecular Evolution / ベ-タバレル構造 / 結晶構造 / 結晶化 |
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| Research Abstract |
1. Structure Analysis of Flammulina veltipes Agglutinin(FVA)Crystal structure of FVA has been refined to an R-factor of 18.7% at 2 A resolution by using the programs XPLOR and PROLSQ. FVA is composed of anti-parallel 7-stranded beta-sheet possessing immunoglobulin fold and a 3-turn alpha-helix at the N-terminus. The structural similarity with immunoglobulin suggests a possibility of the evolutional relationship of this protein with it.
2. Crystallization of Chicken beta-galactoside Binding Lectin This protein crystallized in space group P2_12_12_1 with a=106.3, b=67.3 and c=44.8 A. with 2 molecules in the asymmetric unit from ammonium sulfate solution at pH 7. The crystal diffracts beyond 2.8 A resolution.
3. Crystallization of S. sieboldiana Lectin of A_2B_2 type subunit association (molecular weight 130000 as a whole)has been tried. We have obtained no good crystal for X-ray diffraction experiments so far. This protein contains considerable amount of carbohydrates and it may hinder the ordered crystallization.
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Report
(3 results)
Research Products
(16 results)
