Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Single-wavelength anomalous dispersion of S atoms (S-SAD) is an elegant phasing method to determine crystal structures that does not require heavy-atom incorporation or selenomethionine derivatization. Nevertheless, this technique has been limited by the paucity of the signal at the usual X-ray wavelengths, requiring very accurate measurement of the anomalous differences. Here, the data collection and structure solution of the N-terminal domain of the ectodomain of HCV E1 from crystals that diffracted very weakly is reported. By combining the data from 32 crystals, it was possible to solve the sulfur substructure and calculate initial maps at 7 Å resolution, and after density modication and phase extension using a higher resolution native data set to 3.5 Å resolution model building was achievable.

Original publication

DOI

10.1107/S139900471401339X

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

08/2014

Volume

70

Pages

2197 - 2203

Keywords

HCV, envelope glycoprotein E1, sulfur SAD, Amino Acid Sequence, Cloning, Molecular, Hepacivirus, Molecular Sequence Data, Protein Conformation, Viral Envelope Proteins