High-resolution Structure of a Retroviral Capsid Domain
Solved at SRS PX Station 14.2

Retroviruses are the source of a range of human diseases, including AIDS and certain types of leukaemia. Maturation of newly formed retroviral particles is an essential step in producing infectious virions, including capsid proteins. Researchers from NIMR ( London ) have succeeded is solving the three-dimensional structure of a hexagonal arrangement of capsid molecules from a leukaemia virus. The structure provides new insights into how retroviruses function and suggests possible ways to disrupt viral replication and thus combat diseases such as leukaemia and AIDS.

The crystal structure was solved to a resolution of 1.9 Å using data from a Multi-wavelength Anomalous Dispersion (MAD) experiment on protein crystallography (PX) station 14.2 at the SRS. Three datasets were collected around the selenium absorption edge to a resolution of 2.6 Å. A third, high-resolution (1.9 Å) dataset was also collected on 14.2.

The work features on the front cover of the 23^rd September 2004 issue of Nature and the full reference is:
Gulnahar B. Mortuza, Lesley F. Haire, Anthony Stevens, Stephen J. Smerdon, Jonathan P. Stoye and Ian A. Taylor. (2004). High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature, 431, 481-485.

 

First Results from New PX Beamline MAD10 - September 2004  

Dr. Fusinita van den Ent and Dr. Jan Lowe (LMB-MRC) were the first users to solve a structure using the Multi-wavelength Anomalous Dispersion (MAD) capability of SRS beamline 10.1. They collected three-wavelength data around the selenium absorption edge overnight on Friday and by the evening of the following Sunday they were able to state 'The structure is basically solved. The native is 2.8 Å we couldn't get anything better, but that should be enough. The density is gorgeous!'

First paper published for work carried out on beamline 10

A group of researchers from Oxford University are the first to publish a paper including data collected on beamline 10.1. Datasets were collected using X-rays of 1.8 Å wavelength to exploit the anomalous signal of manganese present in the protein. The data were collected in May 2004 and published in the journal Cell in September 2004. The full reference is:

Mancini, E.J., Kainov, D.E., Grimes, J.M.,Tuma, R., Bamford, D.H. and Stuart, D.I. (2004). Atomic Snapshots of an RNA Packaging Motor Reveal Conformational Changes Linking ATP Hydrolysis to RNA Translocation. Cell, 118 (6), 743-755.

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