Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 65, Issue -, Pages 849-852Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109027900
Keywords
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Funding
- NIH Center of Biomedical Research Excellence in Molecular Targets [5P20 RR 018733, R01GM079516]
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Smc5/6, a protein complex that belongs to the structural maintenance of chromosome (SMC) family, plays a key role in DNA replication, sister chromatid recombination and DNA damage repair. The complex contains eight subunits, including a SUMO E3 ligase Mms21 (Nse2). The activity of Mms21 is important for regulation of Smc5/6 in the response to DNA damage. Mms21 and the Mms21-binding region of Smc5 were overexpressed and purified individually in Escherichia coli with a C-terminal LEHHHHHH tag. The Mms21-Smc5 protein complex was crystallized. The diffraction of the crystals was improved greatly by glutaraldehyde treatment. X-ray diffraction data sets were collected to resolutions of 2.3 and 3.9 angstrom from native and selenomethionine-derivative protein crystals, respectively. The crystals belonged to space group C222(1), with unit-cell parameters a = 47.465, b = 97.574, c = 249.215 angstrom for the native crystals.
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