. 2016 Feb 26;291(18):9785–9795. doi: 10.1074/jbc.M115.696591

TABLE 3.

Summary of hydrodynamic properties of DAPDC enzymes

DAPDC	Oligomer	Theoretical molecular mass^a	s_20,^w	Experimental molecular mass^b	f/f₀^c	K_D^2→1^d
		kDa	S	kDa		nm
B. anthracis	Dimer	98	5.6	83	1.3	ND^e
E. coli	Monomer	47	4.2	52	1.1	ND
	Dimer	94	5.5	81	1.4
M. tuberculosis	Monomer	50	3.7	50	1.3	ND
	Dimer	100	5.4	86	1.4
V. cholerae	Dimer	98	5.6	92	1.3	ND
V. cholerae labeled (Abs)	Dimer	100	5.8	98	1.3	ND
V. cholerae	Monomer	50	3.6	41	1.3	0.06
labeled (FDS)	Dimer	100	5.6	91	1.3
N381A	Monomer	49	3.6	46	1.2	17.3
	Dimer	98	5.1	76	1.4
R385A	Monomer	49	3.7	51	1.2	410
	dimer	98	5.2	77	1.4

^a Molecular masses derived from amino acid sequence.

^b Molecular masses obtained from the ordinate maximum of peaks in the c(M) distribution.

^c Frictional ratio derived using the v̄ bar method (24).

^d Determined from global nonlinear best fit to a monomer-dimer equilibrium model using sedimentation equilibrium data at multiple concentrations and rotor speeds.

^e ND, not determined.