Table 1.

MS-crosslinks identified in the lipid free apoA-I dimer, and Lys-Lys distances, corresponding to these MS-crosslinks, measured in the model of lipid free apoA-I dimer.

MS-xlinka	Silva et al.b		Pollard et al.c		Segrest et al.d
	Observede	Distancef [Å]	Observed	Distance [Å]	Observed	Distance [Å]
Nt–Nt	√	22.4		58.9		12.7
Nt–K77	√	48.1		31.5		39.2
		50.0		31.0		38.1
Nt–Kg118		22.6	√	52.5		42.3
		24.9		50.8		44.5
Nt–K238	√	16.2		46.7		13.5
		18.0		46.2		17.0
K88–Kg118		45.0	√	12.0		55.8
		47.6		9.5		57.0
K208–K208	√	33.2		36.0		46.1
K208–K238	√	29.9		47.1		10.7
		31.2		46.0		15.3
K226–K238	√	29.4		29.4		12.0
		30.1		28.1		13.7
K238–K238	√	34.8		31.8		29.9

^aAmino acid residues forming the crosslink.

^bLipid free apoA-I dimer built from Silva et al. lipid free apoA-I monomer model (Silva et al., 2005a).

^cLipid free apoA-I dimer built from Pollard et al. lipid free apoA-I monomer model (Pollard et al., 2013).

^dLipid free apoA-I dimer built from Segrest et al. lipid free apoA-I monomer model (Segrest et al., 2014).

^eThe crosslink is checked if it was experimentally observed in the study that reports the model for the lipid free apoA-I monomer.

^fMinimum distance between the residues involved in the crosslink measured in the lipid free apoA-I dimer model.

^gThis crosslink was reported for an apoA-I concentration of 1 mg/mL but not at 0.2 mg/mL, so it is assumed to form between different apoA-I chains within multimeric lipid free apoA-I (Pollard et al., 2013).