title: Crystallization and preliminary crystallographic analysis of the catalytic domain of human flap endonuclease 1 in complex with a nicked DNA product: use of a DPCS kit for efficient protein-DNA complex crystallization.
abstract: Flap endonuclease 1 (FEN1) is a structure-specific nuclease that removes the RNA/DNA primer associated with Okazaki fragments in DNA replication. Here, crystals of the complex between the catalytic domain of human FEN1 and a DNA product have been obtained. For efficient crystallization screening, a DNA-protein complex crystallization screening (DPCS) kit was designed based on commercial crystallization kits. The crystal was found to belong to space group P2(1), with unit-cell parameters a = 61.0, b = 101.3, c = 106.4 A, beta = 106.4 degrees. The asymmetric unit is predicted to contain two complexes in the crystallographic asymmetric unit. A diffraction data set was collected to a resolution of 2.75 A.
authors: Structural Biology Laboratory, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
authors: Shigeru
authors: S
authors: Sakurai
authors: Ken
authors: K
authors: Kitano
authors: Hiroshi
authors: H
authors: Morioka
authors: Toshio
authors: T
authors: Hakoshima
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D045585:Flap Endonucleases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D014961:X-Ray Diffraction
chemical_list: D004247:DNA; D045585:Flap Endonucleases