Crystallization and preliminary crystallographic studies of the metalloglycoprotein esterase A4 using a baculovirus expression system

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):734-6. doi: 10.1107/S1744309107033854. Epub 2007 Aug 10.

Abstract

Esterase A4 (EA4) is a timer protein found in diapause eggs of the silkworm Bombyx mori. The gene for this metalloglycoprotein was cloned from B. mori eggs and expressed using a baculovirus expression system in silkworm pupae. Crystals of the purified protein have been grown that diffract to beyond 2.1 A resolution at 100 K using synchrotron radiation. The protein crystals belong to space group P2(1), with unit-cell parameters a = 47.1, b = 73.9, c = 47.4 A, beta = 104.1 degrees. With one dimer per asymmetric unit, the crystal volume per unit protein weight (V(M)) is 2.3 A3 Da(-1) and the solvent content is 47%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Baculoviridae
  • Base Sequence
  • Bombyx / enzymology
  • Carboxylesterase / chemistry*
  • Carboxylesterase / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • DNA Primers
  • Female
  • Glycoproteins / chemistry
  • Glycoproteins / isolation & purification
  • Glycosylation
  • Metalloproteins / chemistry
  • Metalloproteins / isolation & purification
  • Molecular Sequence Data
  • Ovum / enzymology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • DNA Primers
  • Glycoproteins
  • Metalloproteins
  • Recombinant Proteins
  • Carboxylesterase