Recurrence of room-temperature measurement in macromolecular crystallography under humidity control

• Kumasaka Takashi

  Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute

• Baba Seiki

  Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute

• Kawamura Takashi

  Protein Crystal Analysis Division, Japan Synchrotron Radiation Research Institute

Bibliographic Information

Other Title

• 結晶調湿Ｘ線回折法と 室温測定の再評価

Abstract

  Protein crystals are generally wet and fragile, thus easily suffer from dehydration and temperature change. To preserve the crystals from such sudden physicochemical conditional changes, we developed a crystal mounting method, humid air and glue coating (HAG) method. This method works well to maintain most protein crystals under both cryogenic and room temperature conditions. Room-temperature measurement has recently advanced in time-resolved analysis by serial femtosecond crystallography (SFX) method using X-ray free electron laser (XFEL) facilities, and emerges dynamical properties of proteins, leading to its recurrence even in synchrotron experiments. Here we show the brief guidance to the method and its application, and discuss the perspective of room-temperature structural analysis in macromolecular crystallography.

Journal

• Journal of the Japanese Association for Crystal Growth

  Journal of the Japanese Association for Crystal Growth 45 (4), n/a-, 2019

  The Japanese Association for Crystal Growth

Details

• CRID: 1390845713050473472
• NII Article ID: 130007585417
• DOI: 10.19009/jjacg.3-45-4-02
• ISSN: 21878366
• ISSN: 03856275
• Text Lang: ja
• Data Source:
  • JaLC
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed