Paper Report for: Gerber_2004_Acta.Crystallogr.D.Biol.Crystallogr_60_531
Reference
Title: Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli Gerber K, Schiefner A, Seige P, Diederichs K, Boos W, Welte W Ref: Acta Crystallographica D Biol Crystallogr, 60:531, 2004 : PubMed
Aes belongs to the family of hormone-sensitive lipases and has acetyl-esterase activity. It is also known to control maltose uptake through interaction with MalT, the central regulator of the Escherichia coli maltose system. Aes was crystallized as an N-terminally His(6)-tagged protein both in the native form and with selenomethionine substitution. Crystals grew in both cases in space group R32 to dimensions of about 0.2 x 0.15 x 0.05 mm (native His(6)-Aes) and about 0.5 x 0.3 x 0.1 mm (SeMet-His(6)-Aes). A native data set has been obtained at 2.4 A resolution; the selenomethionine-substituted Aes crystals diffracted to 3.0 A resolution.
Gerber K, Schiefner A, Seige P, Diederichs K, Boos W, Welte W (2004) Crystallization and preliminary X-ray analysis of Aes, an acetyl-esterase from Escherichia coli Acta Crystallographica D Biol Crystallogr60: 531-3
Gerber K, Schiefner A, Seige P, Diederichs K, Boos W, Welte W (2004) Acta Crystallographica D Biol Crystallogr60: 531-3