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A 1.5 A resolution structure of the C-terminal-truncated monomeric tubulin [alpha,beta, tubulin gammaS (a,b,g)] has been determined. Only minimal differences are seen between the monomeric and dimeric [alpha, beta,gammaS (alpha,beta,gammaS)] tubulin and confirm that the dimerization is driven through the exchange of the gamma-subunit in the crystal. The monomer is similar to the dimer, which shows that the tetramer is formed by the N-terminal domains of the alpha and beta-tubulin only. It is also shown that the tubulin dimer, but
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