Atomic resolution view into the structure–function relationships of the human myelin peripheral membrane protein P2

Ruskamo, S.; Yadav, R.P.; Sharma, S.; Lehtimäki, M.; Laulumaa, S.; Aggarwal, S.; Simons, M.; Bürck, J.; Ulrich, A.S.; Juffer, A.H.; Kursula, I.; Kursula, P.

doi:10.1107/S1399004713027910

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 1
Crystal structure of human P2. (a) Overall structure of human P2. (b) Electron density for the ligands cis-vaccenate (magenta) and palmitate (cyan). The final refined 2F_o − F_c map is contoured at 1.5σ. OMIT maps calculated without palmitate are shown in Supplementary Fig. S2. (c) Orientation of the fatty-acid COOH group. The 2F_o − F_c map (5.5σ) is shown. (d) The difference map, calculated without H atoms (green, 1.7σ; magenta, 2.5σ). The lost proton in Arg106 is indicated by the arrow.

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 1| December 2014| Pages 165-176

doi:10.1107/S1399004713027910

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