Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of human ribosomal protein L7a (RPL7a)

Title
Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of human ribosomal protein L7a (RPL7a)
Author(s)
박현호장태호[장태호]박진희[박진희]전주홍[전주홍]이동섭[이동섭]최기항[최기항]김인규[김인규]김영환[김영환]
Keywords
NOBEL LECTURE; GENES; EXPRESSION; BINDING; RNA
Issue Date
201105
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.67, pp.510 - 512
Abstract
Ribosomal proteins are a major component of ribosomes, which catalyze protein synthesis. One ribosomal protein, L7a (RPL7a), which is a component of the 60S large ribosomal subunit, has additional functions involved in cell growth and differentiation that occur via interaction with human thyroid hormone receptor (THR) and retinoic acid receptor (RAR) and in turn inhibit the activities of the two nuclear hormone receptors. In this study, the N-terminal domain of human RPL7a was overexpressed in Escherichia coli using an engineered C-terminal His tag. The N-terminal domain of human RPL7a was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.5 A from a crystal belonging to the tetragonal space group P4(1)22 or P4(3)22 with unit-cell parameters a = 92.28, b = 92.28, c = 236.59 A.
URI
http://hdl.handle.net/YU.REPOSITORY/25197http://dx.doi.org/10.1107/S1744309111006415
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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