The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 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

PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)

Voltage-dependent anion-selective channel protein 1

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

Rods of dimensions 10x25x150 micrometers

25.5% Precipitant mix 4 [precipitant mix 4 consists of 25% (v/v) MPD, 25% (w/v) PEG1000, 25% (w/v) PEG3350], 0.06M NaNO3, 0.08M K2HPO4, 0.1M Buffer System2 [HEPES and MOPS adjusted to pH 7.5]

software PISA determined the quaternary structure .
Interface area A-B: 828 ANGSTROM**2
Solvation energy A-B: -19 kcal/mol

software PISA determined the quaternary structure .
Interface area C-D: 877 ANGSTROM**2
Solvation energy A-B: -21 kcal/mol

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

binding site for Di-peptide PHE C 103 and LYS C 110