%0 Journal Article
	%A Jun Yop An and  Kyoung Ryoung Park and  Jung-Gyu Lee and  Hyung-Seop Youn and Jung-Yeon Kang and  Gil Bu Kang and  Soo Hyun Eom
	%D 2010
	%J International Journal of Bioengineering and Life Sciences
	%B World Academy of Science, Engineering and Technology
	%I Open Science Index 44, 2010
	%T X-ray Crystallographic Analysis of MinC N-Terminal Domain from Escherichia coli
	%U https://publications.waset.org/pdf/5731
	%V 44
	%X MinC plays an important role in bacterial cell division
system by inhibiting FtsZ assembly. However, the molecular
mechanism of the action is poorly understood. E. coli MinC Nterminus
domain was purified and crystallized using 1.4 M sodium
citrate pH 6.5 as a precipitant. X-ray diffraction data was collected
and processed to 2.3 Å from a native crystal. The crystal belonged to
space group P212121, with the unit cell parameters a = 52.7, b = 54.0,
c = 64.7 Å. Assuming the presence of two molecules in the
asymmetric unit, the Matthews coefficient value is 1.94 Å3 Da-1,
which corresponds to a solvent content of 36.5%. The overall
structure of MinCN is observed as a dimer form through anti-parallel
ß-strand interaction.
	%P 516 - 519