Open AccessExpression, purification and preliminary crystallographic studies of a single‐point mutant of Mos1 mariner transposase
Author(s) -
Richardson Julia M.,
Zhang Lei,
Marcos Severine,
Finnegan David J.,
Harding Marjorie M.,
Taylor Paul,
Walkinshaw Malcolm D.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904003798
Subject(s) - transposase , mutant , crystallography , crystallization , escherichia coli , tetragonal crystal system , chemistry , resolution (logic) , biology , transposable element , gene , genetics , crystal structure , computer science , organic chemistry , artificial intelligence
A soluble single‐point mutant of full‐length Mos1 mariner transposase (MW = 40.7 kDa) has been overexpressed in Escherichia coli , purified to 95% homogeneity and crystallized. This provides the first example of the crystallization of a eukaryotic transposase. The native crystals diffract to 2.5 Å resolution and show tetragonal symmetry, with unit‐cell parameters a = b = 44.5, c = 205.6 Å. Multiple‐wavelength anomalous data from a selenomethionyl form of the protein and data from a heavy‐atom derivative have been collected.