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Crystallization and preliminary X-ray studies of the pectate lyase from Bacillus subtilis.

作者信息

Jenkins J, Nasser W, Scott M, Pickersgill R, Vignon J C, Robert-Baudouy J

机构信息

Department of Protein Engineering, AFRC Institute of Food Research, Reading, U.K.

出版信息

J Mol Biol. 1992 Dec 20;228(4):1255-8. doi: 10.1016/0022-2836(92)90330-m.

Abstract

The pectate lyase (EC 4.2.2.9) from Bacillus subtilis has been crystallized. Crystals of form 1, grown by the hanging drop method using polyethylene glycol as precipitant, diffract to at least 2.4 A resolution. They belong to the spacegroup P2(1) with a = 132.9 A, b = 41.2 A, c = 156.8 A and beta = 114.9 degrees with probably four molecules in the asymmetric unit. A second crystal form grown from 2-methyl-2,4-pentandiol also belongs to the spacegroup P2(1) with a = 55.0 A, b = 88.1 A, c = 50.2 A and beta = 109.0 degrees. These crystals diffract to at least 2.0 A and have one molecule in the asymmetric unit. Both crystal forms are suitable for the determination of high-resolution structures.

摘要

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