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A technique for high-throughput protein crystallization in ionically cross-linked polysaccharide gel beads for X-ray diffraction experiments.

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  • المؤلفون: Sugahara M;Sugahara M
  • المصدر:
    PloS one [PLoS One] 2014 Apr 16; Vol. 9 (4), pp. e95017. Date of Electronic Publication: 2014 Apr 16 (Print Publication: 2014).
  • نوع النشر :
    Journal Article; Research Support, Non-U.S. Gov't
  • اللغة:
    English
  • معلومة اضافية
    • المصدر:
      Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
    • بيانات النشر:
      Original Publication: San Francisco, CA : Public Library of Science
    • الموضوع:
      Gels/*chemistry ; Polysaccharides/*chemistry ; Proteins/*chemistry ; X-Ray Diffraction/*methods; Alginates/chemistry ; Carrageenan/chemistry ; Cross-Linking Reagents/chemistry ; Crystallization/methods ; Glucuronic Acid/chemistry ; Hexuronic Acids/chemistry ; Hot Temperature ; Ions/chemistry ; Muramidase/chemistry ; Reproducibility of Results ; Zeolites/chemistry
    • نبذة مختصرة :
      A simple technique for high-throughput protein crystallization in ionically cross-linked polysaccharide gel beads has been developed for contactless handling of crystals in X-ray crystallography. The method is designed to reduce mechanical damage to crystals caused by physical contact between crystal and mount tool and by osmotic shock during various manipulations including cryoprotection, heavy-atom derivatization, ligand soaking, and diffraction experiments. For this study, protein crystallization in alginate and κ-carrageenan gel beads was performed using six test proteins, demonstrating that proteins could be successfully crystallized in gel beads. Two complete diffraction data sets from lysozyme and ID70067 protein crystals in gel beads were collected at 100 K without removing the crystals; the results showed that the crystals had low mosaicities. In addition, crystallization of glucose isomerase was carried out in alginate gel beads in the presence of synthetic zeolite molecular sieves (MS), a hetero-epitaxic nucleant; the results demonstrated that MS can reduce excess nucleation of this protein in beads. To demonstrate heavy-atom derivatization, lysozyme crystals were successfully derivatized with K2PtBr6 within alginate gel beads. These results suggest that gel beads prevent serious damage to protein crystals during such experiments.
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    • الرقم المعرف:
      0 (Alginates)
      0 (Cross-Linking Reagents)
      0 (Gels)
      0 (Hexuronic Acids)
      0 (Ions)
      0 (Polysaccharides)
      0 (Proteins)
      1318-02-1 (Zeolites)
      8A5D83Q4RW (Glucuronic Acid)
      9000-07-1 (Carrageenan)
      EC 3.2.1.17 (Muramidase)
    • الموضوع:
      Date Created: 20140418 Date Completed: 20150207 Latest Revision: 20211021
    • الموضوع:
      20250114
    • الرقم المعرف:
      PMC3989300
    • الرقم المعرف:
      10.1371/journal.pone.0095017
    • الرقم المعرف:
      24740192