Toggle Main Menu Toggle Search

Open Access padlockePrints

Going soft and SAD with manganese

Lookup NU author(s): Professor Paula SalgadoORCiD


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.

Publication metadata

Author(s): Salgado PS, Walsh MA, Laurila MRL, Stuart DI, Grimes JM

Publication type: Article

Publication status: Published

Journal: Acta Biol Crystallographica D

Year: 2005

Volume: D61

Issue: 1

Pages: 108-111

ISSN (print): 0907-4449

ISSN (electronic): 1399-0047

Publisher: Wiley-Blackwell Publishing, Inc.


DOI: 10.1107/S0907444904026800

PubMed id: 15608382


Altmetrics provided by Altmetric