Open AccessCrystallization and initial X‐ray analysis of polyhydroxyalkanoate granule‐associated protein from Aeromonas hydrophila
Author(s) -
Zhao Minglian,
Li Zhenguo,
Lou Zhiyong,
Zheng Wei,
Chen GuoQiang
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106025000
Subject(s) - polyhydroxyalkanoates , granule (geology) , aeromonas hydrophila , crystallization , bacteria , chemistry , crystallography , materials science , biology , genetics , organic chemistry , composite material
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 80.8, b = 108.9, c = 134.4 Å .