The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 2.7 Angstrom resolution

The dynamic nature of the VDAC1 channels in bilayers as revealed by two crystal structures of the human isoform in bicelles at 2.7 and 3.3 Angstrom resolution: implications for VDAC1 voltage-dependent mechanism and for its oligomerization

Voltage-dependent anion-selective channel protein 1

hVDAC1,Outer mitochondrial membrane protein porin 1,Plasmalemmal porin,Porin 31HL,Porin 31HM

plates of sizes 10 x 30 x 30 micrometers

25.5% precipitant mix 4 [25% (v/v) MPD, 25% (w/v) PEG 1000, 25% (w/v) PEG 3350], 0.06 M NH4NO3, 0.1 buffer system 1 [imidazole and MES adjusted to pH 6.5]

software PISA determined the quaternary structure .
Interface area A-B: 1118 ANGSTROM**2
Solvation energy A-B: -24.5 kcal/mol

ion-channel, B-barrel, outer mitochondrial membrane, cytochrome c release, APOPTOSIS, transport protein