The orientation of a <i>T</i> = 1 assembly of alfalfa mosaic virus coat protein in a hexagonal crystalline array

Abdel-Meguid, Sherin S.; Fukuyama, Keiichi; Rossmann, Michael G.

doi:10.1107/s0567740882007754

Cited by 6 publications

(4 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Rotation function analysis of the new data set was in agreement with that obtained by Abdel-Meguid et al (2). The two virus particles are situated in the P6 3 hexagonal cell with their threefold icosahedral axes coincident with the crystal threefold axes and are related to each other by the crystal twofold screw axis.…”

Section: Resultssupporting

confidence: 88%

“…The present structure confirms the analysis of Fukuyama et a AMV diffraction data were collected on a GX20 Elliott rotating anode X-ray generator using oscillation photography by Fita et al (11). Film processing indexing, and postrefinement of the data were earlier reported (2) and have been repeated with improved versions of the programs to obtain a better-quality data set. Rotation function and crystal packing analyses were also repeated and were found to agree with the previously reported results (2).…”

Section: Resultsmentioning

confidence: 99%

“…Film processing indexing, and postrefinement of the data were earlier reported (2) and have been repeated with improved versions of the programs to obtain a better-quality data set. Rotation function and crystal packing analyses were also repeated and were found to agree with the previously reported results (2). An initial set of phases for data between 20 and 15 Å was computed from the model built by Fita et al (11), using the program X-PLOR (6).…”

Section: Resultsmentioning

confidence: 99%

“…X-ray crystallographic studies of this Tϭ1 particle were undertaken in the early 1980s when 4.5-Å diffraction data were obtained from crystals of the truncated particles (2,13). The electron density map that was obtained with phases computed by the single isomorphous replacement method and subsequent averaging using 20-fold noncrystallographic symmetry revealed a spherical particle about 210 Å in diameter and with prominent holes (ϳ38 Å in diameter) at the icosahedral fivefold axes (12).…”

mentioning

confidence: 99%

See 3 more Smart Citations

The structure of alfalfa mosaic virus capsid protein assembled as a T=1 icosahedral particle at 4.0-A resolution

Kumar

Reddy

Yusibov

et al. 1997

J Virol

View full text Add to dashboard Cite

reported the structure of alfalfa mosaic virus assembled from the capsid protein as a T‫1؍‬ icosahedral empty particle at 4.5-Å resolution. The information contained in the structure included the particle size, protein shell thickness, presence of wide holes at the icosahedral fivefold axes, and a proposal that the capsid protein adopts a ␤-barrel structure. In the present work, the X-ray diffraction data of Fukuyama et al. as well as the data subsequently collected by I. Fita, Y. Hata, and M. G. Rossmann (unpublished) were reprocessed to 4.0-Å resolution, and the structure was solved by molecular replacement. The current structure allowed the tracing of the polypeptide chain of the capsid protein confirming the ␤-sandwich fold and provides information on intersubunit interactions in the particle. However, it was not possible to definitively assign the amino acid sequence to the side chain density at 4-Å resolution. The particle structure was also determined by cryoelectron microscopy and image reconstruction methods and found to be in excellent agreement with the X-ray model.

show abstract

Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%