3wdn
From Proteopedia
High-resolution X-ray crystal structure of bovine H-protein using a high-pressure cryocooling method
Structural highlights
FunctionGCSH_BOVIN The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. Publication Abstract from PubMedRecently, 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 A 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. High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method.,Higashiura A, Ohta K, Masaki M, Sato M, Inaka K, Tanaka H, Nakagawa A J Synchrotron Radiat. 2013 Nov;20(Pt 6):989-93. doi: 10.1107/S090904951302373X., Epub 2013 Oct 5. PMID:24121354[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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