Apocrustacyanin A1 from the lobster carotenoprotein alpha-crustacyanin: crystallization and initial X-ray analysis involving softer X-rays.
The A1 subunit of the carotenoprotein alpha-crustacyanin, isolated from lobster carapace, has been crystallized using the vapour-diffusion method. The crystals, grown in solutions of ammonium sulfate containing methylpentanediol (MPD), diffracted to 2. 0 A. The crystals are stable to radiation. The space group of the crystals is P2(1)2(1)2(1). The unit-cell parameters are a = 41.9, b = 80.7, c = 110.8 A. 'Standard structure determination' has been unsuccessful within this crustacyanin family. Instead, an approach based on the S atoms is being undertaken involving softer X-rays at the SRS, Daresbury.
Chayen
N E
NE
Biological Structure and Function Section, Division of Biomedical Sciences, Imperial College School of Medicine, London SW7 2AZ, England.
Cianci
M
M
Olczak
A
A
Raftery
J
J
Rizkallah
P J
PJ
Zagalsky
P F
PF
Helliwell
J R
JR
D000818:Animals; D001059:Apoproteins / Q000737:chemistry / Q000302:isolation & purification; D002352:Carrier Proteins; D003460:Crystallization; D018360:Crystallography, X-Ray; D008121:Nephropidae; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification
D001059:Apoproteins; D002352:Carrier Proteins; D011506:Proteins; C018494:crustacyanins