1CWP

STRUCTURES OF THE NATIVE AND SWOLLEN FORMS OF COWPEA CHLOROTIC MOTTLE VIRUS DETERMINED BY X-RAY CRYSTALLOGRAPHY AND CRYO-ELECTRON MICROSCOPY

Summary for 1CWP

• Entry DOI: 10.2210/pdb1cwp/pdb
• Descriptor: RNA (5'-R(*AP*UP*AP*U)-3'), RNA (5'-R(*AP*U)-3'), Coat protein (3 entities in total)
• Functional Keywords: bromovirus, icosahedral virus, virus-rna complex, virus/rna
• Biological source: Cowpea chlorotic mottle virus
• Total number of polymer chains: 6
• Total formula weight: 64050.74

Authors

Speir, J.A.,Johnson, J.E.,Munshi, S.,Wang, G.,Timothy, S.,Baker, T.S. (deposition date: 1995-05-22, release date: 1995-05-22, Last modification date: 2024-02-14)

Primary citation

Speir, J.A.,Munshi, S.,Wang, G.,Baker, T.S.,Johnson, J.E.
Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy.
Structure, 3:63-77, 1995

PubMed Abstract: RNA-protein interactions stabilize many viruses and also the nucleoprotein cores of enveloped animal viruses (e.g. retroviruses). The nucleoprotein particles are frequently pleomorphic and generally unstable due to the lack of strong protein-protein interactions in their capsids. Principles governing their structures are unknown because crystals of such nucleoprotein particles that diffract to high resolution have not previously been produced. Cowpea chlorotic mottle virions (CCMV) are typical of particles stabilized by RNA-protein interactions and it has been found that crystals that diffract beyond 4.5 A resolution are difficult to grow. However, we report here the purification of CCMV with an exceptionally mild procedure and the growth of crystals that diffract X-rays to 3.2 A resolution.

PubMed: 7743132
DOI: 10.1016/S0969-2126(01)00135-6

Experimental method

X-RAY DIFFRACTION (3.2 Å)