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Gertrud Beterams, Bettina Böttcher, M. Nassal (2000)
Packaging of up to 240 subunits of a 17 kDa nuclease into the interior of recombinant hepatitis B virus capsidsFEBS Letters, 481
P. Plevka, K. Tārs, L. Liljas (2008)
Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particlesProtein Science, 17
D. Koletzki, A. Zankl, H. Gelderblom, H. Meisel, A. Dišlers, G. Borisova, P. Pumpens, D. Krüger, R. Ulrich (1997)
Mosaic hepatitis B virus core particles allow insertion of extended foreign protein segments.The Journal of general virology, 78 ( Pt 8)
K. Valegård, T. Unge, I. Montelius, B. Strandberg, W. Fiers (1986)
Purification, crystallization and preliminary X-ray data of the bacteriophage MS2.Journal of molecular biology, 190 4
B. Matthews (1968)
Solvent content of protein crystals.Journal of molecular biology, 33 2
B. Böttcher, M. Vogel, M. Ploss, M. Nassal (2006)
High plasticity of the hepatitis B virus capsid revealed by conformational stress.Journal of molecular biology, 356 3
Adam Zlotnick, I. Palmer, J. Kaufman, S. Stahl, A. Steven, P. Wingfield (1999)
Separation and crystallization of T = 3 and T = 4 icosahedral complexes of the hepatitis B virus core protein.Acta crystallographica. Section D, Biological crystallography, 55 Pt 3
S. Wynne, R. Crowther, A. Leslie (1999)
The crystal structure of the human hepatitis B virus capsid.Molecular cell, 3 6
(2006)
Scaling and assessment of data quality
Kyung-mi Choi, Seung-Hye Choi, Hyesun Jeon, In‐San Kim, H. Ahn (2011)
Chimeric capsid protein as a nanocarrier for siRNA delivery: stability and cellular uptake of encapsulated siRNA.ACS nano, 5 11
D. Peabody, F. Lim (1996)
Complementation of RNA binding site mutations in MS2 coat protein heterodimers.Nucleic acids research, 24 12
R. Crowther, N. Kiselev, Bettina Böttcher, J. Berriman, G. Borisova, V. Ose, P. Pumpens (1994)
Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopyCell, 77
(1999)
Acta Cryst
Fan Yang, L. Moss, G. Phillips (1996)
The molecular structure of green fluorescent proteinNature Biotechnology, 14
T. Douglas, M. Young (2006)
Viruses: Making Friends with Old FoesScience, 312
Evans (2006)
10.1107/S0907444905036693Acta Cryst. D, 62
T. Battye, Luke Kontogiannis, O. Johnson, H. Powell, A. Leslie (2011)
iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLMActa Crystallographica Section D: Biological Crystallography, 67
A. Vagin, A. Teplyakov (2010)
Molecular replacement with MOLREP.Acta crystallographica. Section D, Biological crystallography, 66 Pt 1
M. Winn, C. Ballard, K. Cowtan, E. Dodson, P. Emsley, P. Evans, R. Keegan, E. Krissinel, A. Leslie, A. Mccoy, S. McNicholas, G. Murshudov, N. Pannu, E. Potterton, H. Powell, R. Read, A. Vagin, K. Wilson (2011)
Overview of the CCP4 suite and current developmentsActa Crystallographica Section D: Biological Crystallography, 67
Claudia Skamel, M. Ploss, B. Böttcher, T. Stehlé, R. Wallich, M. Simon, M. Nassal (2006)
Hepatitis B Virus Capsid-like Particles Can Display the Complete, Dimeric Outer Surface Protein C and Stimulate Production of Protective Antibody Responses against Borrelia burgdorferi Infection*Journal of Biological Chemistry, 281
M. Vogel, M. Diez, J. Eisfeld, M. Nassal (2005)
In vitro assembly of mosaic hepatitis B virus capsid‐like particles (CLPs): Rescue into CLPs of assembly‐deficient core protein fusions and FRET‐suited CLPsFEBS Letters, 579
K. Diederichs, P. Karplus (1997)
Improved R-factors for diffraction data analysis in macromolecular crystallographyNature Structural Biology, 4
P. Tiollais, P. Charnay, G. Vyas (1981)
Biology of hepatitis B virus.Science, 213 4506
S. French, K. Wilson (1978)
On the treatment of negative intensity observationsActa Crystallographica Section A, 34
R. Higuchi, B. Krummel, R. Saiki (1988)
A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions.Nucleic acids research, 16 15
P. Singh, Maria Gonzalez, M. Manchester (2006)
Viruses and their uses in nanotechnologyDrug Development Research, 67
A. Zlotnick, N. Cheng, S. Stahl, J. Conway, A. Steven, P. Wingfield (1997)
Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: implications for morphogenesis and organization of encapsidated RNA.Proceedings of the National Academy of Sciences of the United States of America, 94 18
Recombinant hepatitis B virus core proteins dimerize to form building blocks that are capable of self‐assembly into a capsid. A core capsid protein dimer (CPD) linked to a green fluorescent protein variant, EGFP, at the C‐terminus has been designed. The recombinant fusion CPD was expressed in Escherichia coli, assembled into virus‐like particles (VLPs), purified and crystallized. The single crystal diffracted to 2.15 Å resolution and belonged to the cubic space group F432, with unit‐cell parameters a = b = c = 219.7 Å. The fusion proteins assembled into icosahedral VLPs in aqueous solution, but were rearranged into octahedral symmetry through the crystal‐packing process under the crystallization conditions.
Acta Crystallographica Section F – Wiley
Published: Feb 1, 2013
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