X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain.
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 Å from a crystal belonging to space group I4, with unit-cell parameters a = 41.95, b = 41.95, c = 318.78 Å. The asymmetric unit was estimated to contain two molecules.
Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
Hyun Ho
HH
Park
D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009687:Nuclear Proteins / Q000737:chemistry* / Q000302:isolation & purification; D017434:Protein Structure, Tertiary
D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C489753:SYCP1 protein, human
SYCP1; coiled-coil domain; crystallization; meiosis; syneptonemal complex