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Purification, crystallization and preliminary X‐ray crystallographic analysis of the flagellar accessory protein FlaH from the methanogenic archaeon Methanocaldococcus jannaschii
Author(s) -
Meshcheryakov Vladimir A.,
Yoon YoungHo,
Matsunami Hideyuki,
Wolf Matthias
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14019980
Subject(s) - crystallization , crystallography , crystal (programming language) , biology , crystal structure , flagellum , protein crystallization , chemistry , biochemistry , gene , organic chemistry , computer science , programming language
The flagellar accessory protein FlaH is thought to be one of the essential components of an archaeal motility system. However, to date biochemical and structural information about this protein has been limited. Here, the crystallization of FlaH from the hyperthermophilic archaeon Methanocaldococcus jannaschii is reported. Protein crystals were obtained by the vapour‐diffusion method. These crystals belonged to space group P 3 1 21, with unit‐cell parameters a = b = 131.42, c = 89.35 Å. The initial solution of the FlaH structure has been determined by multiple‐wavelength anomalous dispersion phasing using a selenomethionine‐derivatized crystal.