Lookup NU author(s): Dr Paula Salgado
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
SAD phasing has been revisited recently, with experiments being carried out using previously unconventional sources of anomalous signal, particularly lighter atoms and softer X-rays. A case study is reported using the 75 kDa RNA-dependent RNA polymerase of the bacteriophase [varphi]6, which binds a Mn atom and crystallizes with three molecules in the asymmetric unit. X-ray diffraction data were collected at a wavelength of 1.89 Å and although the calculated anomalous signal from the three Mn atoms was only 1.2%, SHELXD and SOLVE were able to locate these atoms. SOLVE/RESOLVE used this information to obtain SAD phases and automatically build a model for the core region of the protein, which possessed the characteristic features of the right-hand polymerase motif. These results demonstrate that with modern synchrotron beamlines and software, manganese phasing is a practical tool for solving the structure of large proteins.
Author(s): Salgado PS, Walsh MA, Laurila MRL, Stuart DI, Grimes JM
Publication type: Article
Publication status: Published
Journal: Acta Biol Crystallographica D
ISSN (print): 0907-4449
ISSN (electronic): 1399-0047
Publisher: Wiley-Blackwell Publishing, Inc.
PubMed id: 15608382
Altmetrics provided by Altmetric