3WDN
High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method
Summary for 3WDN
| Entry DOI | 10.2210/pdb3wdn/pdb |
| Descriptor | Glycine cleavage system H protein, mitochondrial, GLYCEROL (3 entities in total) |
| Functional Keywords | antiparallel beta sheet, beta sandwich, oxidoreductase |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Mitochondrion: P20821 |
| Total number of polymer chains | 1 |
| Total formula weight | 14042.56 |
| Authors | Higashiura, A.,Nakagawa, A. (deposition date: 2013-06-19, release date: 2013-10-30, Last modification date: 2023-11-08) |
| Primary citation | Higashiura, A.,Ohta, K.,Masaki, M.,Sato, M.,Inaka, K.,Tanaka, H.,Nakagawa, A. High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method J.SYNCHROTRON RADIAT., 20:989-993, 2013 Cited by PubMed Abstract: 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. PubMed: 24121354DOI: 10.1107/S090904951302373X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.86 Å) |
Structure validation
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