Crystal structure of the yellow 1:2 molecular complex lumiflavin–bisnaphthalene-2,3-diol

In the first molecular complex of the physiologically active neutral form of isoalloxazine studied, lumiflavin–bisnaphthalene-2,3-diol, each flavin is sandwiched between two naphthalenediol molecules with extensive overlap but a moderately large (3·44 Å) spacing, indicating at most weak charge-transfer interaction and in agreement with the yellow colour of the complex, nearly the same as that of the parent lumiflavin

Heterodimers as the Structural Unit of the T=1 Capsid of the Fungal Double-Stranded RNA Rosellinia Necatrix Quadrivirus 1

Most double-stranded RNA (dsRNA) viruses are transcribed and replicated in a specialized icosahedral capsid with a T=1 lattice consisting of 60 asymmetric capsid protein (CP) dimers. These capsids help to organize the viral genome and replicative complex(es). They also act as molecular sieves that isolate the virus genome from host defense mechanisms and allow the passage of nucleotides and viral transcripts. Rosellinia necatrix quadrivirus 1 (RnQV1), the type species of the family Quadriviridae, is a dsRNA fungal virus with a multipartite genome consisting of four monocistronic segments (segments 1 to 4). dsRNA-2 and dsRNA-4 encode two CPs (P2 and P4, respectively), which coassemble into ∼450-Å-diameter capsids. We used three-dimensional cryo-electron microscopy combined with complementary biophysical techniques to determine the structures of RnQV1 virion strains W1075 and W1118. RnQV1 has a quadripartite genome, and the capsid is based on a single-shelled T=1 lattice built of P2-P4 dimers. Whereas the RnQV1-W1118 capsid is built of full-length CP, P2 and P4 of RnQV1-W1075 are cleaved into several polypeptides, maintaining the capsid structural organization. RnQV1 heterodimers have a quaternary organization similar to that of homodimers of reoviruses and other dsRNA mycoviruses. The RnQV1 capsid is the first T=1 capsid with a heterodimer as an asymmetric unit reported to date and follows the architectural principle for dsRNA viruses that a 120-subunit capsid is a conserved assembly that supports dsRNA replication and organization

Trus, “Multi-channel restoration of electron micrographs

We introduce a projection based multi-channel restoration method which is useful in cases for which there is no a priori information about the input signal. The method is especially helpful in situations where a large number of specimens are later combined to achieve additional noise reduction. We describe the approach and discuss the problem of restoring electron micrographs. The method does require knowledge of the impulse response of the degradation. For this reason, the sensitivity of the approach to uncertainty in this degradation is investigated through simulation. 1

Structure and Polymorphism of the UL6 Portal Protein of Herpes Simplex Virus Type 1

By electron microscopy and image analysis, we find that baculovirus-expressed UL6 is polymorphic, consisting of rings of 11-, 12-, 13-, and 14-fold symmetry. The 12-mer is likely to be the oligomer incorporated into procapsids: at a resolution of 16 Å, it has an axial channel, peripheral flanges, and fits snugly into a vacant vertex site. Its architecture resembles those of bacteriophage portal/connector proteins

Handedness of the Herpes Simplex Virus Capsid and Procapsid

The capsid of herpes simplex virus has an icosahedral surface lattice with a nonskew triangulation number, T=16. Nevertheless, the proteins arrayed on this lattice necessarily have an intrinsic handedness. We have determined the handedness of both the herpes simplex virus type 1 capsid and its precursor procapsid by a cryoelectron microscopic tilting method