Open AccessIsolation, purification, crystallization and preliminary X‐ray studies of two 30 kDa proteins from silkworm haemolymph
Author(s) -
Pietrzyk Agnieszka J.,
Bujacz Anna,
Łochyńska Małgorzata,
Jaskólski Mariusz,
Bujacz Grzegorz
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110054564
Subject(s) - hemolymph , bombyx mori , orthorhombic crystal system , crystallography , triclinic crystal system , crystallization , molecular mass , biology , instar , biochemistry , chemistry , larva , enzyme , botany , crystal structure , organic chemistry , gene
Juvenile hormone‐binding protein (JHBP) and the low‐molecular‐mass lipoprotein PBMHP‐12 belong to a group of 30 kDa proteins that comprise the major protein component of the haemolymph specific to the fifth‐instar larvae stage of the mulberry silkworm Bombyx mori L. Proteins from this group are often essential for the development of the insect. In a project aimed at crystallographic characterization of B. mori JHBP (BmJHBP), it was copurified together with PBMHP‐12. Eventually, the two proteins were isolated and crystallized separately. The BmJHBP crystals were orthorhombic (space group C 222 1 ) and the PBMHP‐12 crystals were triclinic. The crystals diffracted X‐rays to 2.9 Å (BmJHBP) and 1.3 Å (PBMHP‐12) resolution.