M. K. Lyon

Details der Publikationsliste

Zeitraum

1998 - 1998

Anzahl

5

Co-Autoren

Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly (1998)

Li, M., Beard, P., Estes, P. A., Lyon, M. K., Garcea, R. L.

In order to analyze bonding contacts that stabilize the virion or promote capsid assembly, bovine papillomavirus (BPV) virions were subjected to buffer conditions known to disrupt polyomavirus...

Expression of the human papillomavirus type 11 L1 capsid protein in Escherichia coli: characterization of protein domains involved in DNA binding and capsid assembly.

Li, M, Cripe, T P, Estes, P A, Lyon, M K, Rose, R C, Garcea, R L

The L1 major capsid protein of human papillomavirus type 11 (HPV-11) was expressed in Escherichia coli, and the soluble recombinant protein was purified to near homogeneity. The recombinant L1...

Direct observation of defect structure in protein crystals by atomic force and transmission electron microscopy.

Devaud, G, Furcinitti, P S, Fleming, J C, Lyon, M K, Douglas, K

We have examined the structure of S-layers isolated from Sulfolobus acidocaldarius using atomic force microscopy (AFM) and transmission electron microscopy (TEM). From the AFM images, we were able to...

Expression of the human papillomavirus type 11 L1 capsid protein in Escherichia coli: characterization of protein domains involved in DNA binding and capsid assembly.

Li, M, Cripe, T P, Estes, P A, Lyon, M K, Rose, R C, Garcea, R L

The L1 major capsid protein of human papillomavirus type 11 (HPV-11) was expressed in Escherichia coli, and the soluble recombinant protein was purified to near homogeneity. The recombinant L1...

Direct observation of defect structure in protein crystals by atomic force and transmission electron microscopy.

Devaud, G, Furcinitti, P S, Fleming, J C, Lyon, M K, Douglas, K

We have examined the structure of S-layers isolated from Sulfolobus acidocaldarius using atomic force microscopy (AFM) and transmission electron microscopy (TEM). From the AFM images, we were able to...