Volume 65, Issue 10 pp. 1065-1067

Cloning, purification and preliminary X-ray crystallographic analysis of a hypothetical protein, MJ0754, from Methanococcus jannaschii DSM 2661

Eun Hye Lee

Eun Hye Lee

Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea

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Ki Hyun Nam

Ki Hyun Nam

Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea

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Kwang Yeon Hwang

Kwang Yeon Hwang

Division of Biotechnology, College of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea

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First published: 22 October 2009
Citations: 1
Kwang Yeon Hwang, e-mail: [email protected]

Abstract

The protein encoded by the MJ0754 gene from the archaeon Methanococcus jannaschii DSM 2661 is an unknown hypothetical protein. Two recombinant proteins, MJ0754 (residues 1–185) and MJ0754t (a truncated form of MJ0754, residues 11–185), were cloned from MJ0754, overexpressed as His-tag fusion proteins and purified. The crystals were found to grow under two different conditions and to have two different shapes. The crystal of MJ0754 belonged to space group P61, with unit-cell parameters a = b = 127.015, c = 48.929 Å, a calculated Matthews coefficient of 2.85 Å3 Da−1 and two molecules per asymmetric unit. The crystal of MJ0754t belonged to space group C2221, with unit-cell parameters a = 51.915, b = 79.122, c = 93.869 Å, a calculated Matthews coefficient of 2.41 Å3 Da−1 and one molecule per asymmetric unit. The SeMet-labelled P61 crystal diffracted to a resolution of 3.1 Å, while the native C2221 crystal diffracted to 1.3 Å resolution.

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