Peter Krijgsman

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Influenza A (X31) virus was purified over a zonal sucrose gradient. The resulting gradient fractions were examined by electron microscopy, HA and infectivity titrations and gel electrophoresis. The fractions containing a homogeneous suspension of spherical particles had the highest infectivity per amount of viral protein and a much higher HA:M ratio than(More)
The stability of the quaternary structure of bottom and top components of alfalfa mosaic virus (respectively AMV-B and AMV-Ta-t) in the pH range 5.5 to 7.8 and at ionic concentrations of 0.01 and 0.1 M has been investigated using small-angle X-ray scattering and photon correlation spectroscopy. The X-ray scattering curves show no significant changes over(More)
The states of aggregation of alfalfa mosaic virus (AMV) protein have been characterized by sedimentation velocity experiments and electron microscopy. The main association product is a spherical particle with an s value of about 30S. It is highly likely that the assembly of this particle starts with dimers of the 25000 molecular mass unit resulting in an(More)
Neutron-scattering in combination with quasi-elastic light-scattering and electron microscopy was used to derive a model for the capsid structure of the Top a-t component of alfalfa mosaic virus (AMV-Ta-t). In the electron microscope, AMV-Ta-t appears as an irregular ellipsoidal particle with apparent dimensions 275 (+/- 31) A X 225 (+/- 22) A. Assuming(More)
Transposition of the E.coli bacteriophage Mu requires the phage encoded A and B proteins, the host protein UU and the host replication proteins. The ends of the genome of the phage, on which some of these proteins act, both contain three transposase (A) binding sites. The organization of these binding sites on each end, however, is different. Here we show,(More)
Transposition of the E. coli bacteriophage Mu requires the phage encoded A and B proteins, the host protein HU and the host replication proteins. The ends of the genome of the phage, on which some of these proteins act, both contain three transposase (A) binding sites. The organization of these binding sites on each end, however, is different. Here we show,(More)
The polymerization of alfalfa mosaic virus (AMV) protein in the presence of homologous nucleic acids and a number of other natural and synthetic nucleic acids was studied. The conditions for optimal assembly were found to be pH 6.0 and low ionic strength (I = 0.1 M) at room temperature, irrespective of the type of nucleic acid. The resulting nucleoprotein(More)
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