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Updated: Aug 6, 2026
Protein Crystallization for X-ray Crystallography
Published on: January 16, 2011
Crystallization and initial X-ray analysis of polyhydroxyalkanoate granule-associated protein from Aeromonas
Minglian Zhao1, Zhenguo Li, Wei Zheng
1MOE Key Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Abstract:
Polyhydroxyalkanoate (PHA) granule-associated proteins (phasins) were discovered in PHA-accumulating bacteria. They play a crucial role as a structural protein during initial PHA-granule formation and granule growth and also serve as interfaces for granule stabilization in vivo. The phasin PhaP(Ah) from Aeromonas hydrophila strain 4AK4 was crystallized using the hanging-drop vapour-diffusion method. Single crystals were cryocooled for X-ray diffraction analysis. The phasin crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 80.8, b = 108.9, c = 134.4 angstroms.
