Crystallization properties and structure of Panulirus interruptus haemocyanin.
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.
Wichertjes
T
T
Biochemisch Laboratorium, Rijksuniversiteit Groningen.
Keegstra
W
W
Neuteboom
B
B
Hazes
B
B
Beintema
J J
JJ
van Bruggen
E F
EF
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D006433:Hemocyanins / Q000302:isolation & purification / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008121:Nephropidae; D011487:Protein Conformation; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D006433:Hemocyanins