Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the Bag2 amino‐terminal domain from Mus musculus
Author(s) -
Page Richard C.,
Xu Zhen,
Amick Joseph,
Nix Jay C.,
Misra Saurav
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112013267
Subject(s) - crystallography , chemistry , dimer , crystallization , x ray crystallography , resolution (logic) , diffraction , physics , computer science , optics , organic chemistry , artificial intelligence
Bag2, an atypical member of the Bag family of Hsp70 co‐chaperones, acts as both an Hsp70 nucleotide‐exchange factor and an inhibitor of the Hsp70‐binding E3 ubiquitin ligase CHIP ( c arboxyl‐terminus of H sp70‐ i nteracting p rotein). The amino‐terminal domain of Bag2 (Bag2‐NTD), which is required for inhibition of CHIP, has no sequence homologs in the PDB. Native and selenomethionyl (SeMet) forms of Bag2‐NTD were crystallized by hanging‐drop vapor diffusion. Native Bag2‐NTD crystals diffracted to 2.27 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 75.5, b = 84.7, c = 114.1 Å. SeMet Bag2‐NTD crystals diffracted to 3.10 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 37.2, b = 53.3, c = 86.7 Å. Phases for the SeMet Bag2‐NTD crystal were solved by single‐wavelength anomalous diffraction. Initial phasing and model building using the 3.10 Å resolution SeMet Bag2‐NTD data set suggested that Bag2‐NTD forms a dimer and adopts a fold distinct from those of any domains annotated in the Pfam or SMART domain databases.