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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.

SUBMITTER: Kang GB 

PROVIDER: S-EPMC2864684 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori.

Kang Gil Bu GB   Song Hye Eun HE   Kim Mun Kyoung MK   Youn Hyung Seop HS   An Jun Yop JY   Lee Jung Gyu JG   Park Kyung Ryung KR   Eom Soo Hyun SH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100429 Pt 5


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(  ...[more]

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