Open AccessCrystallization of a 79 kDa fragment of the hook protein FlgE from Campylobacter jejuni
Author(s) -
Kido Yasuji,
Yoon YoungHo,
Samatey Fadel A.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111043272
Subject(s) - monoclinic crystal system , resolution (logic) , crystallography , crystallization , tetragonal crystal system , crystal (programming language) , campylobacter jejuni , chemistry , crystal structure , biology , bacteria , genetics , organic chemistry , artificial intelligence , computer science , programming language
A 79 kDa fragment of the bacterial flagellar hook protein FlgE from Campylobacter jejuni was cloned, overexpressed, purified and crystallized. Two different crystal forms were obtained. Synchrotron X‐ray diffraction data showed that the first crystal form, which diffracted to 4.9 Å resolution, belonged to the tetragonal crystal system, with space group I 4 1 22 and unit‐cell parameters a = b = 186.2, c = 386.6 Å, α = β = γ = 90°. The second crystal form diffracted to 2.5 Å resolution and belonged to the monoclinic crystal system, with space group P 2 1 and unit‐cell parameters a = 75.7, b = 173.8, c = 150.8 Å, α = γ = 90, β = 106.5°. SeMet protein was also overexpressed, purified and crystallized, and a 2.6 Å resolution MAD data set was collected.