Open AccessCrystallization and preliminary X‐ray diffraction of the first periplasmic domain of SecDF, a translocon‐associated membrane protein, from Thermus thermophilus
Author(s) -
Echizen Yuka,
Tsukazaki Tomoya,
Dohmae Naoshi,
Ishitani Ryuichiro,
Nureki Osamu
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111031885
Subject(s) - thermus thermophilus , periplasmic space , translocon , crystallography , crystallization , transmembrane protein , transmembrane domain , biophysics , membrane , chemistry , membrane protein , biology , biochemistry , escherichia coli , receptor , organic chemistry , gene
A membrane‐integrated Sec component, SecDF, associates with the SecYEG protein‐conducting channel and facilitates protein secretion and membrane–protein integration. SecDF contains 12 transmembrane helices and two periplasmic domains. The first periplasmic domain (P1) plays an important role in protein translocation. Here, the overexpression, purification and crystallization of the P1 domain of Thermus thermophilus SecDF are reported. The crystals diffracted X‐rays to 2.3 Å resolution and belonged to space group C 2, with unit‐cell parameters a = 161.1, b = 35.8, c = 181.6 Å, suggesting that they contain four molecules per asymmetric unit. The initial phases were determined by the multiple‐wavelength anomalous dispersion method using selenomethionine‐labelled crystals.