Farley MM, Tu J, Kearns DB, Molineux IJ, Liu J (2017) Ultrastructural analysis of bacteriophage Φ29 during infection of Bacillus subtilis. J Struct Biol 197:163–171 All entered vectors and their sum are also plotted on the graph below the results, so you can see the graphical result of the operation, where the vector sum is shown in red. The vector sum is plotted by placing vectors head to tail and drawing the vector from the free tail to the free head (so-called Parallelogram law).

The BAP hexamer has overall outer dimensions of ∼150 × 100 Å, similar to previous structures of ClpB/Hsp104 ( Parsell et al., 1994; Lee et al., 2003; Wendler et al., 2007, 2009; Figure 1C). It encloses a ∼30 Å wide central channel, comparable in size to that in the crystal structure of ClpC ( Wang et al., 2011; Figure 1C,D). In the reconstruction it is possible to identify regions accounting for all the domains, such as L-shaped densities for the AAA+ domains and a rod-like density for the coiled-coil MD.The cephalocaudal trend is often contrasted with proximodistal development which refers to growth that occurs from the center of the body outward towards its periphery. This type of growth is seen in infants as they learn how to move arms before they can control fine finger movement. The cephalocaudal principle is the idea that development proceeds from the head down to the tail, or top to bottom. This means that the earliest changes during development will occur in the head and facial areas, and then progress downwards towards the rest of the body. For example, a newborn baby might develop their eyes before their legs. Step 3. If there are more than two vectors, continue this process for each vector to be added. Note that in our example, we have only two vectors, so we have finished placing arrows tip to tail.

Motwani T, Lokareddy RK, Dunbar CA, Cortines JR, Jarrold MF, Cingolani G, Teschke CM (2017) A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly. Sci Adv 3:e1700423 The middle domains are known to form coiled-coils, with protein helices coiled together like the strands of a rope. However, previous efforts to work out the structure of the ClpB complex did not clearly establish where these coiled-coils were positioned relative to the rest of the ring. Nováček J, Šiborová M, Benešík M, Pantůček R, Doškař J, Plevka P (2016) Structure and genome release of Twort-like Myoviridae phage with a double-layered baseplate. Proc Natl Acad Sci U S A 113:9351–9356We disagree that an ADP-bound subunit is more similar to an empty state than to an ATP-bound one. HX experiments of ClpB did not reveal differences in protection patterns in ADP and ATPγS, arguing that the conformations are similar [Oguchi, Y, et al, Nat Struct Mol Biol, 2012]. Importantly, both ADP and ATPγS binding led to substantial increase in HX protection compared to nucleotide-free ClpB oligomers, including Walker A motif regions. These data indicate that the overall conformational state of ADP-bound ClpB is more similar to the ATP-bound state than to the empty one. Thomas JO, Sternberg N, Weisberg R (1978) Altered arrangement of the DNA in injection-defective lambda bacteriophage. J Mol Biol 123:149–161 Casjens S, Hendrix R (1988) Control mechanisms in dsDNA bacteriophage assembly. In: Calendar R (ed) The bacteriophages, vol 1. Plenum Press, New York Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR (2002) The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. J Mol Biol 318:1395–1404