Open AccessCrystallization and preliminary crystallographic studies of the metalloglycoprotein esterase A4 using a baculovirus expression system
Author(s) -
Hiraki Toshiki,
Shibayama Naoya,
Yoon YoungHo,
Yun KyungMook,
Hamamoto Toshiro,
Tame Jeremy R. H.,
Park SamYong
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107033854
Subject(s) - bombyx mori , crystallization , crystallography , esterase , resolution (logic) , dimer , protein crystallization , chemistry , biology , microbiology and biotechnology , gene , biochemistry , enzyme , organic chemistry , artificial intelligence , computer science
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 Å resolution at 100 K using synchrotron radiation. The protein crystals belong to space group P 2 1 , with unit‐cell parameters a = 47.1, b = 73.9, c = 47.4 Å, β = 104.1°. With one dimer per asymmetric unit, the crystal volume per unit protein weight ( V M ) is 2.3 Å 3 Da −1 and the solvent content is 47%.