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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(67), p. 892-895, 2011

DOI: 10.1107/s1744309111022858

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Crystallization and X-ray diffraction analysis of nylon-oligomer hydrolase (NylC) fromAgromycessp. KY5R

Journal article published in 2011 by Kengo Yasuhira, Naoki Shibata, Yasuhito Tanaka, Naoya Kumagai, Yusuke Tanaka, Keisuke Nagai, Dai-Ichiro Kato, Masahiro Takeo, Seiji Negoro ORCID, Yoshiki Higuchi
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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Abstract

6-Aminohexanoate-oligomer hydrolase (NylC) from Agromyces sp. KY5R was expressed in Escherichia coli JM109 and purified by ammonium sulfate fractionation, anion-exchange column chromatography and gel-filtration chromatography. NylC was crystallized by the sitting-drop vapour-diffusion method with sodium citrate as a precipitant in 0.1 M HEPES buffer pH 7.5 containing 0.2 M NaCl. Diffraction data were collected from native and K(2)PtCl(4)-derivative crystals to resolutions of 2.00 and 2.20 Å, respectively. The obtained crystal was plate-shaped, with an I-centred orthorhombic space group and unit-cell parameters a = 155.86, b = 214.45, c = 478.80 Å. The anomalous difference Patterson map of the K(2)PtCl(4)-derivative crystal suggested that the space group was I222 rather than I2(1)2(1)2(1).