Crystallization and preliminary X-ray crystallographic analysis of MinE, the cell-division topological specificity factor from Helicobacter pylori.
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.
Kang
Gil Bu
GB
Department of Life Science, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
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
D001426:Bacterial Proteins / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000737:chemistry*
D001426:Bacterial Proteins; D018797:Cell Cycle Proteins
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