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Crystallization and preliminary X-ray crystallographic analysis of Z-ring-associated protein (ZapD) from Escherichia coli.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Feb2015, Vol. 71 Issue 2, p194-198, 5p
- Publication Year :
- 2015
-
Abstract
- 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 P6<subscript>4</subscript>, 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<subscript>M</subscript>) of 3.25 Å<superscript>3</superscript> Da<superscript>−1</superscript> and a solvent content of 62.17%. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 71
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 100952711
- Full Text :
- https://doi.org/10.1107/S2053230X15000266