Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction.

ABSTRACT: The study of micro- or nanocrystalline proteins by magic-angle spinning (MAS) solid-state NMR (SSNMR) gives atomic-resolution insight into structure in cases when single crystals cannot be obtained for diffraction studies. Subtle differences in the local chemical environment around the protein, including the characteristics of the cosolvent and the buffer, determine whether a protein will form single crystals. The impact of these small changes in formulation is also evident in the SSNMR spectra; however, the changes lead only to correspondingly subtle changes in the spectra. Here, we demonstrate that several formulations of GB1 microcrystals yield very high quality SSNMR spectra, although only a subset of conditions enable growth of single crystals. We have characterized these polymorphs b

SUBMITTER: Schmidt HL 

PROVIDER: S-EPMC2774121 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature