Open AccessCrystallization properties and structure of Panulirus interruptus haemocyanin
Author(s) -
WICHERTJES Trijntje,
KEEGSTRA Wilko,
NEUTEBOOM Ben,
HAZES Bart,
BEINTEMA Jaap J.,
BRUGGEN Ernst F. J.
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb15018.x
Subject(s) - crystallization , protein subunit , crystallography , electron microscope , diffraction , sequence (biology) , similarity (geometry) , materials science , biology , chemistry , physics , computer science , image (mathematics) , optics , thermodynamics , biochemistry , artificial intelligence , gene
Electron‐microscopic studies revealed that two types of subunits of Panulirus interruptus haemocyanin crystallize in different ways. Homohexamers of subunit a give close‐packed two‐dimensional crystals whereas homohexamers of subunit c form open two‐dimensional arrays. We applied computer‐image analysis to these arrays and studied the differences in crystallization properties by combining the electron‐microscopic data with amino acid sequence information and the X‐ray diffraction model of subunit a .