Given a question and a context passage, generate the answer having the word or phrase from the context passage. Here, the answer should be a shortest continous span from the passage.

Ex Input:
Context: Between 1911 and 1912, over 1,000 Somalis from Mogadishu, the then capital of Italian Somaliland, served as combat units along with Eritrean and Italian soldiers in the Italo-Turkish War. Most of the troops stationed never returned home until they were transferred back to Italian Somaliland in preparation for the invasion of Ethiopia in 1935. The first disembarkation of Italian troops occurred on October 10. The Italian contingent of 20,000 troops was deemed sufficient to accomplish the conquest at the time. Tobruk, Derna and Khoms were easily conquered, but the same was not true for Benghazi. The first true setback for the Italian troops happened on October 23, when poor placement of the troops near Tripoli led them to be almost completely encircled by more mobile Arab cavalry, backed by some Turkish regular units. The attack was portrayed as a simple revolt by the Italian press, but it nearly annihilated much of the small Italian expeditionary corps. The corps was consequently enlarged to 100,000 men who had to face 20,000 Arabs and 8,000 Turks. The war turned into one of position. Even some of the earliest examples of utilisation in modern warfare of armoured cars and air power by the Italian forces had little effect on the initial outcome. However, the war was notable for the first military use of heavier-than-air craft. Capitano Carlo Piazza flew the first military reconnaissance flight on 23 October 1911. A week later, Sottotenente Giulio Gavotti dropped four grenades on Taguira and Ain Zara in history's first aerial bombing. 
 Question: Aerial bombing by who?

Ex Output:
giulio gavotti


Ex Input:
Context: Human erythrocyte spectrin is an antiparallel heterodimer comprised of a 280 kDa alpha subunit and a 246 kDa beta subunit which further associates into tetramers in the red cell membrane cytoskeleton. Lateral association of the flexible rodlike monomers involves a multiple-step process that is initiated by a high affinity association near the actin-binding end of the molecule (dimer nucleation site). In this study, recombinant alpha and beta proteins comprising two or four "spectrin type" motifs with and without adjacent, terminal nonhomologous domains were evaluated for their relative contributions to dimer initiation, and the thermodynamic properties of these heterodimer complexes were measured. Sedimentation equilibrium studies showed that in the absence of the heterologous subunit, individual recombinant proteins formed weak homodimers (K(d) > 0.3 mM). When 2-motif (alpha20-21 and beta1-2) and 4-motif (alpha18-21 and beta1-4) recombinants lacking the terminal nonhomologous domains were paired with the complementary protein, high affinity heterodimers were formed in sedimentation equilibrium analysis. Both the alpha20-21/beta1-2 complex and the alpha20-21EF/betaABD1-2 complex showed stoichiometric binding with similar binding affinities (K(d) approximately 10 nM) using isothermal titration calorimetry. The alpha20-21/beta1-2 complex showed an enthalpy of -10 kcal/mol, while the alpha20-21EF/betaABD1-2 complex showed an enthalpy of -13 kcal/mol. Pull-down assays using alpha spectrin GST fusion proteins showed strong associations between all heterodimer complexes in physiological buffer, but all heterodimer complexes were destabilized by the presence of Triton X-100 and other detergents. Complexes lacking the nonhomologous domains were destabilized to a greater extent than complexes that included the nonhomologous domains. The detergent effect appears to be responsible for the apparent essential role of the nonhomologous domains in prior reports. Taken together, our results indicate that the terminal nonhomologous domains do not contribute to dimer initiation nor are they required for formation of high affinity spectrin heterodimers in physiological buffers. 
 Question: Alpha-spectrin and beta-spectrin subunits form parallel or antiparallel heterodimers?

Ex Output:
antiparallel


Ex Input:
Context: Methylation of lysine residues in the N-terminal tails of histones is thought to represent an important component of the mechanism that regulates chromatin structure. The evolutionarily conserved SET domain occurs in most proteins known to possess histone lysine methyltransferase activity. We present here the crystal structure of a large fragment of human SET7/9 that contains a N-terminal beta-sheet domain as well as the conserved SET domain. Mutagenesis identifies two residues in the C terminus of the protein that appear essential for catalytic activity toward lysine-4 of histone H3. Furthermore, we show how the cofactor AdoMet binds to this domain and present biochemical data supporting the role of invariant residues in catalysis, binding of AdoMet, and interactions with the peptide substrate. 
 Question: What is the characteristic domain of histone methyltransferases?

Ex Output:

set domain