The Helicobacter pylori GroES Cochaperonin HspA Functions as a Specialized Nickel Chaperone and Sequestration Protein through Its Unique C-Terminal Extension -- Schauer et al. 192 (5): 1231 Data Supplement - Supplemental material -- The Journal of Bacteriology

The Helicobacter pylori GroES Cochaperonin HspA Functions as a Specialized Nickel Chaperone and Sequestration Protein through Its Unique C-Terminal Extension
J. Bacteriol. Schauer et al. 192: 1231

Supplemental material

Files in this Data Supplement:

Supplemental file 1 - Fig. S1, comparison of HspA proteins from H. pylori 26695 and H. acinonychis strain Sheeba
Zipped PDF file, 48K.
Supplemental file 2 - Fig. S2, immunoblots of H. pylori 26695 and hspA-C mutant whole-cell lysates
Zipped PDF file, 114K.
Supplemental file 3 - Fig. S3, growth of 26695 and its hspA-ΔC mutant in liquid Brucella broth medium with β-cyclodextrin
Zipped PDF file, 101K.
Supplemental file 4 - Fig. S4, mouse colonizing experiment with H. pylori wild-type strain X47-2AL and the isogenic hspA-C mutant
Zipped PDF file, 70K.
Supplemental file 5 - Table S1, oligonucleotides
MS Word document, 125K.