Crystallization and preliminary X-ray crystallographic studies of cPOP1

Title
Crystallization and preliminary X-ray crystallographic studies of cPOP1
Author(s)
박현호도경훈
Keywords
PROTEIN; INFLAMMASOME; APOPTOSIS
Issue Date
201303
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.69, pp.292 - 294
Abstract
Cellular pyrin domain-only protein 1 (cPOP1) is a pyrin domain (PYD)-containing protein that can regulate inflammation by preventing the assembly of inflammasome via direct interaction with ASC (apoptosis-associated speck-like protein containing a caspase recruitment domain). In this study, cPOP1, corresponding to amino acids 187, was overexpressed in Escherichia coli using an engineered C-terminal polyhistidine tag. cPOP1 was then purified to homogeneity and crystallized at 293K. Finally, X-ray diffraction data were collected to a resolution of 3.6 angstrom from a crystal belonging to the cubic space group P213 with unit-cell parameters a = b = c = 94.12 angstrom, = = = 90.00 degrees.
URI
http://hdl.handle.net/YU.REPOSITORY/26224http://dx.doi.org/10.1107/S1744309113002686
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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