Open AccessCloning, purification and preliminary X‐ray crystallographic analysis of a hypothetical protein, MJ0754, from Methanococcus jannaschii DSM 2661
Author(s) -
Lee Eun Hye,
Nam Ki Hyun,
Hwang Kwang Yeon
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109036562
Subject(s) - methanococcus , cloning (programming) , crystallography , chemistry , materials science , biochemistry , gene , computer science , escherichia coli , programming language
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 P 6 1 , with unit‐cell parameters a = b = 127.015, c = 48.929 Å, a calculated Matthews coefficient of 2.85 Å 3 Da −1 and two molecules per asymmetric unit. The crystal of MJ0754t belonged to space group C 222 1 , with unit‐cell parameters a = 51.915, b = 79.122, c = 93.869 Å, a calculated Matthews coefficient of 2.41 Å 3 Da −1 and one molecule per asymmetric unit. The SeMet‐labelled P 6 1 crystal diffracted to a resolution of 3.1 Å, while the native C 222 1 crystal diffracted to 1.3 Å resolution.