High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method

Recently, many technical improvements in macromolecular X-ray crystallography have increased the number of structures deposited in the Protein Data Bank and improved the resolution limit of protein structures. Almost all high-resolution structures have been determined using a synchrotron radiation s...

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Veröffentlicht in:Journal of synchrotron radiation. - 1994. - 20(2013), Pt 6 vom: 07. Nov., Seite 989-93
1. Verfasser: Higashiura, Akifumi (VerfasserIn)
Weitere Verfasser: Ohta, Kazunori, Masaki, Mika, Sato, Masaru, Inaka, Koji, Tanaka, Hiroaki, Nakagawa, Atsushi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Journal of synchrotron radiation
Schlagworte:Journal Article Research Support, Non-U.S. Gov't H-protein high-pressure cryocooling method high-resolution X-ray crystallography Proteins
Beschreibung
Zusammenfassung:Recently, many technical improvements in macromolecular X-ray crystallography have increased the number of structures deposited in the Protein Data Bank and improved the resolution limit of protein structures. Almost all high-resolution structures have been determined using a synchrotron radiation source in conjunction with cryocooling techniques, which are required in order to minimize radiation damage. However, optimization of cryoprotectant conditions is a time-consuming and difficult step. To overcome this problem, the high-pressure cryocooling method was developed (Kim et al., 2005) and successfully applied to many protein-structure analyses. In this report, using the high-pressure cryocooling method, the X-ray crystal structure of bovine H-protein was determined at 0.86 Å resolution. Structural comparisons between high- and ambient-pressure cryocooled crystals at ultra-high resolution illustrate the versatility of this technique. This is the first ultra-high-resolution X-ray structure obtained using the high-pressure cryocooling method
Beschreibung:Date Completed 22.05.2014
Date Revised 10.11.2023
published: Print-Electronic
PDB: 3WDN
Citation Status MEDLINE
ISSN:1600-5775
DOI:10.1107/S090904951302373X