Crystal structure reveals conservation of amyloid-β conformation recognized by 3D6 following humanization to bapineuzumab

Table 1 Crystallographic data statistics

	3D6Aβ1-7	3D6Aβ1-40
Space group	C2	P222₁
Unit cell lengths (Å)	a = 126.8	a = 40.0
angles (°)	b = 69.4	b = 84.9
	c = 61.7	c = 175.9
	β = 115.4
Resolution Å(last shell)	2.0 (2.05)	2.2 (2.26)
R_sym(last shell)^a	6.5 (23.0)	5.9 (18.9)
Mean((I)/σ(I))	15.0 (5.0)	19.9 (7.9)
% completeness (last shell)	100 (100)	100 (100)
Average multiplicity	3.8 (3.7)	5.8 (5.9)
Residues in final model (total)	1-218 (219)	1-204,
Light chain	1–132,	207–216 (219)
Heavy chain	140–219 (222)	1–100, 103–132,
		140–219 (222)
	1-6
Aβ		1-5
R_free ^a	20.4	22.7
R^a	15.8	17.7
Average B (Å²)	28.5	29.4
Bond length RMSD (Å)	0.007	0.008
Angle RMSD (°)	1.1	1.2
Ramachandran plot: (% in preferred/ allowed/ outliers regions)^b	97.2/2.8/0.0	95.8/3.9/0.3

^aRsym = ∑ _h ∑ _I(| I_i(h) - < I(h) > |) /∑h ∑ _iI_i(h) where I_i(h) = observed intensity, and < I(h) > = mean intensity obtained from multiple measurements. R and R_free = ∑ h|F_o(h) - F_c(h)| /∑_hF_o(h), where F_o(h) = observed structure factor amplitude and F_c(h) = calculated structure factor amplitude for the working and test sets, respectively. ^bAs defined in Coot. RMSD, root mean square deviation of atomic position.

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