Table 1.

Comparison of the Cβ–Cβ distances (in Å) in the crystal structures of the closed and open states and after MD relaxation with fused MAM, along with the end-to-end distances for the free MAM in solution^a.

DOI: http://dx.doi.org/10.7554/eLife.11050.012

	Horizontal cross-linking		Vertical cross-linking
State/isomer	closed/cis	open/trans	closed/trans	open/cis
X-Ray	16.1	27.7	20.8	23.2
Free MAM MD △ from X-Ray	16.0 ± 4.6 -0.1b	21.7 ± 2.0 -6.0	21.7 ± 2.0 0.9	16.0 ± 4.6 -7.2
Fused MAM MD △ from X-Ray	17.1 ± 0.5 +1.0	24.7 ± 0.6 -3.0	18.9 ± 0.9 -1.9	17.2 ± 1.0 -6.0

^aThe distances are measured between the Cβ atoms of the native or cysteine-cross-linked residues, that is, I336(C) for horizontal cross-linking and I336(C)/N353(C) for vertical cross-linking, or between the S atoms for the free MAM. ^bNote that in this case, ∆ gives only an estimate of the difference because it was determined from the S-S distances of free MAM and Cβ–Cβ distances of the X-ray data.

MD: Molecular dynamics; MAM: 4,4´-bis(maleimido-glycine)azobenzene.