| 1. |
- Axblom, C, et al.
(författare)
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Structure of phage fr capsids with a deletion in the FG loop: Implications for viral assembly
- 1998
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Ingår i: VIROLOGY. - : ACADEMIC PRESS INC. - 0042-6822. ; 249:1, s. 80-88
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- The loop between beta-strands F and G in the coat protein of small RNA bacteriophages forms the interactions at the fivefold and threefold (quasi-sixfold) icosahedral axes. In many cases, mutations in this region renders the coat protein unable to form ca
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| 2. |
- Golmohammadi, R, et al.
(författare)
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The crystal structure of bacteriophage Q beta at 3.5 angstrom resolution
- 1996
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Ingår i: STRUCTURE. - : CURRENT BIOLOGY LTD. - 0969-2126. ; 4:5, s. 543-554
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this in
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| 3. |
- Tars, K, et al.
(författare)
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Structure determination of bacteriophage PP7 from Pseudomonas aeroginosa: from poor data to a good map
- 2000
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Ingår i: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. - : MUNKSGAARD INT PUBL LTD. - 0907-4449. ; 56, s. 398-405
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Tidskriftsartikel (refereegranskat)abstract
- The structure of bacteriophage PP7 from Pseudomomas aeruginosa was determined to 3.7 Angstrom resolution. Triclinic crystals of three forms were obtained, diffracting to between 4.5 and 3.4 Angstrom resolution. The quality of the crystals was exceptionall
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| 4. |
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| 5. |
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