STRUCTURE AND PROPERTIES OF H1 CRUSTACYANIN FROM LOBSTER HOMARUS AMERICANUS

Structural Characterization of Recombinant Crustacyanin Subunits from the Lobster Homarus Americanus.

DKIPDFVVPGKCASVTRNKLWAEQTPNRNMYAGVWYQFALTNNPYQLIEKCVRNEYSFDGEQFVITSTGIAYDGNLLKRN
GKLYPNPFGEPHLSIDYEMSFAAPLVILETDYSNYACLYSCIDYNFGYHSDFSFIFSRSANLADKYVKKCEAAFKNINVD
TTRFVKTVQGSSCPYDTQKTV

CRYSTALLIZATION CONDITIONS: H1 PROTEIN SOLUTION AT 10.7 MG/ML IN TRIS-HCL 0.1M, PH 7.0, AND EDTA 1MM WAS USED IN CRYSTALLIZATION EXPERIMENTS. THE BEST CRYSTALS WERE GROWN BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION WITH EDTA 1MM, 2.4 M AMMONIUM SULPHATE, 5% V/V 2-METHYL-2,4-PENTANEDIOL (MPD) AND TRIS-HCL PH 8.0 BUFFER. CRYSTALS GREW IN A WEEK TO A SIZE OF 100 BY 30 BY 30 MICROMETERS.

THE CRYSTAL STRUCTURE OF LOBSTER APOCRUSTACYANIN A1 USING SOFTER X-RAYS.

APOCRUSTACYANIN C1 CRYSTALS GROWN IN SPACE AND EARTH USING VAPOUR DIFFUSION GEOMETRY

THE STRUCTURE AND REFINEMENT OF APOCRUSTACYANIN C2 TO 1.3ARESOLUTION AND THE SEARCH FOR DIFFERENCES BETWEEN THISPROTEIN AND THE HOMOLOGOUS APOPROTEINS A1 AND C1

SEQUENCE MATCHED TO CLOSEST UNIPROT ENTRY. THERE IS A GENBANK REFERENCE FOR THIS ENTRY DV771534

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY

TRANSPORT PROTEIN, CHROMOPHORE BINDING PROTEIN, BATHOCHROMIC SHIFT, ASTAXANTHIN, COLOURATION, RECOMBINANT CAROTENOPROTEINS, CARAPACE