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Crystallization and preliminary X‐ray crystallographic analysis of Z‐ring‐associated protein (ZapD) from Escherichia coli
Author(s) -
Son Sang Hyeon,
Lee Hyung Ho
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15000266
Subject(s) - ftsz , cytokinesis , crystallography , crystallization , escherichia coli , polymerization , tubulin , chemistry , monomer , ring (chemistry) , polyethylene glycol , cell division , stereochemistry , microtubule , biology , biochemistry , cell , organic chemistry , gene , microbiology and biotechnology , polymer
Bacterial cytokinesis is accomplished by the Z‐ring, which is a polymeric structure that includes the tubulin homologue FtsZ at the division site. ZapD, a Z‐ring‐associated protein, directly binds to FtsZ and stabilizes the polymerization of FtsZ to form a stable Z‐ring during cytokinesis. Structural analysis of ZapD from Escherichia coli was performed to investigate the mechanism of ZapD‐mediated FtsZ stabilization and polymerization. ZapD was crystallized using a reservoir solution consisting of 1.5 M lithium sulfate, 0.1 M HEPES pH 7.8, 2%( v / v ) polyethylene glycol 400. X‐ray diffraction data were collected to 2.95 Å resolution. The crystals belonged to the hexagonal space group P 6 4 , with unit‐cell parameters a = b = 109.5, c = 106.7 Å, γ = 120.0°. Two monomers were present in the asymmetric unit, resulting in a crystal volume per protein mass ( V M ) of 3.25 Å 3 Da −1 and a solvent content of 62.17%.