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Crystallization and preliminary X-ray analysis of the periplasmic domain of FliP, an integral membrane component of the bacterial flagellar type III protein-export apparatus.
- Source :
- Acta Crystallographica: Section F, Structural Biology Communications; Sep2014, Vol. 70 Issue 9, p1215-1218, 4p
- Publication Year :
- 2014
-
Abstract
- The bacterial flagellar proteins are transported via a specific export apparatus to the distal end of the growing structure for their self-assembly. FliP is an essential membrane component of the export apparatus. FliP has an N-terminal signal peptide and is predicted to have four transmembrane (TM) helices and a periplasmic domain (FliP<subscript>P</subscript>) between TM-2 and TM-3. In this study, FliP<subscript>P</subscript> from Thermotoga maritima (TmFliP<subscript>P</subscript>) and its selenomethionine derivative (SeMet-TmFliP<subscript>P</subscript>) were purified and crystallized. TmFliP<subscript>P</subscript> formed a homotetramer in solution. Crystals of TmFliP<subscript>P</subscript> and SeMet-TmFliP<subscript>P</subscript> were obtained by the hanging-drop vapour-diffusion technique with 2-methyl-2,4-pentanediol as a precipitant. These two crystals grew in the hexagonal space group P6<subscript>2</subscript>22 or P6<subscript>4</subscript>22, with unit-cell parameters a = b = 114.9, c = 193.8 Å. X-ray diffraction data were collected from crystals of TmFliP<subscript>P</subscript> and SeMet-TmFliP<subscript>P</subscript> to 2.4 and 2.8 Å resolution, respectively. [ABSTRACT FROM AUTHOR]
- Subjects :
- CRYSTALLIZATION
PROTEINS
SELENOMETHIONINE
X-ray diffraction
CRYSTALS
Subjects
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- 9
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 97983149
- Full Text :
- https://doi.org/10.1107/S2053230X14014678