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Isolation, purification, crystallization and preliminary X-ray studies of two 30?kDa proteins from silkworm haemolymph.

ABSTRACT: 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 C222(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.

SUBMITTER: Pietrzyk AJ

PROVIDER: S-EPMC3053166 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Isolation, purification, crystallization and preliminary X-ray studies of two 30 kDa proteins from silkworm haemolymph.

Pietrzyk Agnieszka J AJ Bujacz Anna A Łochyńska Małgorzata M Jaskólski Mariusz M Bujacz Grzegorz G

Acta crystallographica. Section F, Structural biology and crystallization communications 20110225 Pt 3

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 ...[more]

PMID: 21393846

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