X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain

Title
X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain
Author(s)
박현호
Issue Date
201509
Publisher
INT UNION CRYSTALLOGRAPHY
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.71, pp.1131 - 1134
Abstract
The synaptonemal complex is a meiosis-specific complex structure formed at the synapse of homologous chromosomes to hold them together during meiosis. Synaptonemal complex protein 1 (SYCP1) is one of the components of the syneptonemal complex. In this study, the short form of the coiled-coil domain of SYCP1 was overexpressed in Escherichia coli with an engineered C-terminal His tag. The short form of the coiled-coil domain of SYCP1 was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.0 angstrom from a crystal belonging to space group I4, with unit-cell parameters a = 41.95, b = 41.95, c = 318.78 angstrom. The asymmetric unit was estimated to contain two molecules.
URI
http://hdl.handle.net/YU.REPOSITORY/31051http://dx.doi.org/10.1107/S2053230X15012728
ISSN
2053-230X
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이과대학 > 화학생화학부 > Articles
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