title: Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori.
abstract: Cell division in Gram-negative bacteria is driven by the formation of an FtsZ ring at the division site. MinE regulates the proper placement of the FtsZ ring at mid-cell by blocking the inhibitory action of the MinCD complex. Diffraction data were collected at 2.8 A resolution from a native crystal of full-length Helicobacter pylori MinE. The crystal belonged to space group P6(4). Assuming the presence of two molecules in the asymmetric unit, the calculated Matthews coefficient was 2.58 A(3) Da(-1), which corresponds to a solvent content of 52.3%. For MAD phasing, a four-wavelength data set was collected at 3.0 A resolution.
authors.affiliation: Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
authors.forename: Gil Bu
authors.initials: GB
authors.lastname: Kang
authors.forename: Hye Eun
authors.initials: HE
authors.lastname: Song
authors.forename: Mun Kyoung
authors.initials: MK
authors.lastname: Kim
authors.forename: Hyung Seop
authors.initials: HS
authors.lastname: Youn
authors.forename: Jun Yop
authors.initials: JY
authors.lastname: An
authors.forename: Jung Gyu
authors.initials: JG
authors.lastname: Lee
authors.forename: Kyung Ryung
authors.initials: KR
authors.lastname: Park
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D018797:Cell Cycle Proteins
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