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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):372-6. doi: 10.1107/S1744309110054564. Epub 2011 Feb 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bombyx / chemistry*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Hemolymph / chemistry*
  • Insect Proteins / chemistry*
  • Insect Proteins / isolation & purification*
  • Larva / metabolism
  • Lipoproteins / chemistry*
  • Lipoproteins / isolation & purification*
  • Molecular Sequence Data
  • Molecular Weight
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • X-Ray Diffraction

Substances

  • Carrier Proteins
  • Insect Proteins
  • Lipoproteins
  • juvenile hormone-binding protein, insect