Crystallization and initial X-ray analysis of polyhydroxyalkanoate granule-associated protein from Aeromonas hydrophila.
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.
Zhao
Minglian
M
MOE Key Laboratory of Protein Science, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, People's Republic of China.
Li
Zhenguo
Z
Zheng
Wei
W
Lou
Zhiyong
Z
Chen
Guo Qiang
GQ
D000217:Acyltransferases / Q000737:chemistry* / Q000302:isolation & purification; D016980:Aeromonas hydrophila / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D017931:DNA Primers; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D015183:Restriction Mapping; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D000217:Acyltransferases; C077225:poly(3-hydroxyalkanoic acid) synthase