Open AccessCrystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY
Author(s) -
Shepotinovskaya Irina V.,
Focia Pamela J.,
Freymann Douglas M.
Publication year - 2003
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444903016573
Subject(s) - signal recognition particle receptor , gtpase , gtp' , crystallization , ammonium sulfate , crystallography , signal recognition particle , biophysics , thermus aquaticus , chemistry , biology , biochemistry , protein targeting , signal peptide , chromatography , peptide sequence , membrane protein , membrane , escherichia coli , organic chemistry , enzyme , gene
The GTPases Ffh and FtsY are components of the prokaryotic signal recognition particle protein‐targeting pathway. The two proteins interact in a GTP‐dependent manner, forming a complex that can be stabilized by use of the non‐hydrolyzable GTP analog GMPPCP. Crystals of the complex of the NG GTPase domains of the two proteins have been obtained from ammonium sulfate solutions. Crystals grow with several different morphologies, predominately as poorly diffracting plates and needle clusters, but occasionally as well diffracting rods. It has been demonstrated that all forms of the crystals observed contain an intact complex. Diffraction data to 2.0 Å resolution have been measured.