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

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%.

SUBMITTER: Hiraki T

PROVIDER: S-EPMC2376319 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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

Hiraki Toshiki T Shibayama Naoya N Yoon Young-Ho YH Yun Kyung-Mook KM Hamamoto Toshiro T Tame Jeremy R H JR Park Sam-Yong SY

Acta crystallographica. Section F, Structural biology and crystallization communications 20070810 Pt 9

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 ...[more]

PMID: 17768340

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