Buy article online - an online subscription or single-article purchase is required to access this article.
Download citation
Download citation
link to html
The polymerase core of double-stranded (ds) RNA virus provides the molecular machinery for RNA packaging and replication. Procapsid of bacteriophage φ6 constitutes the best studied model of such dsRNA-processing machine. A total of 120 copies of protein P1 form the procapsid framework to which other proteins are attached. Due to their low abundance minor procapsid constituents, P2 (RNA polymerase) and P7 (packaging factor), have not up to now been localized. We have applied small-angle neutron scattering (SANS) and contrast variation in order to localize the two proteins. Procapsids containing deuterated P2 or P7 were produced in vitro and SANS was collected at several contrast levels. Radial positions of labeled proteins were obtained and modeled within the electron density of the procapsid. P2 monomers reside at each five-fold vertex just under the RNA packaging complex. P7 was detected at a distance of 160 Å from the procapsid center indicating localization on the inner surface of P1 framework.

Subscribe to Journal of Applied Crystallography

The full text of this article is available to subscribers to the journal.

If you have already registered and are using a computer listed in your registration details, please email support@iucr.org for assistance.

Buy online

You may purchase this article in PDF and/or HTML formats. For purchasers in the European Community who do not have a VAT number, VAT will be added at the local rate. Payments to the IUCr are handled by WorldPay, who will accept payment by credit card in several currencies. To purchase the article, please complete the form below (fields marked * are required), and then click on `Continue'.
E-mail address* 
Repeat e-mail address* 
(for error checking) 

Format*   PDF (US $40)
In order for VAT to be shown for your country javascript needs to be enabled.

VAT number 
(non-UK EC countries only) 
Country* 
 

Terms and conditions of use
Contact us

Follow J. Appl. Cryst.
Sign up for e-alerts
Follow J. Appl. Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds