A temperature-controlled cold-gas humidifier and its application to protein crystals with the humid-air and glue-coating method

The room-temperature experiment has been revisited for macromolecular crystallography. Despite being limited by radiation damage, such experiments reveal structural differences depending on temperature, and it is expected that they will be able to probe structures that are physiologically alive. For...

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Bibliographische Detailangaben
Veröffentlicht in:Journal of applied crystallography. - 1998. - 52(2019), Pt 4 vom: 01. Aug., Seite 699-705
1. Verfasser: Baba, Seiki (VerfasserIn)
Weitere Verfasser: Shimada, Atsuhiro, Mizuno, Nobuhiro, Baba, Junpei, Ago, Hideo, Yamamoto, Masaki, Kumasaka, Takashi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Journal of applied crystallography
Schlagworte:Journal Article X-ray diffraction glue coating humidity control protein crystals temperature control
Beschreibung
Zusammenfassung:The room-temperature experiment has been revisited for macromolecular crystallography. Despite being limited by radiation damage, such experiments reveal structural differences depending on temperature, and it is expected that they will be able to probe structures that are physiologically alive. For such experiments, the humid-air and glue-coating (HAG) method for humidity-controlled experiments is proposed. The HAG method improves the stability of most crystals in capillary-free experiments and is applicable at both cryogenic and ambient temperatures. To expand the thermal versatility of the HAG method, a new humidifier and a protein-crystal-handling workbench have been developed. The devices provide temperatures down to 4°C and successfully maintain growth at that temperature of bovine cytochrome c oxidase crystals, which are highly sensitive to temperature variation. Hence, the humidifier and protein-crystal-handling workbench have proved useful for temperature-sensitive samples and will help reveal temperature-dependent variations in protein structures
Beschreibung:Date Revised 18.07.2024
published: Electronic-eCollection
Citation Status PubMed-not-MEDLINE
ISSN:0021-8898
DOI:10.1107/S1600576719006435