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![[Figure 4]](wa5138fig4mag.jpg)
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Figure 4
Extrapolated electron-density maps at four different pump–probe time delays calculated using the dark-state model. Extrapolated electron-density maps, ![[2mF_{\rm ext}^{\Delta t\_{\rm light}}]](teximages/wa5138fi37.svg) − ![[DF_{\rm calc}^{\rm dark}]](teximages/wa5138fi13.svg) (1 r.m.s.d., blue) and ![[mF_{\rm ext}^{\Delta t\_{\rm light}}]](teximages/wa5138fi12.svg) − (+3 r.m.s.d., green; −3 r.m.s.d., red), calculated between the light and dark data sets with Δt = 20 ps (a, e), 900 ps (b, f) and 300 ns (c, g) at 2 Å resolution and 2 µs (d, h) at 2.2 Å resolution. Maps are shown around the fatty acid (FA) and Cys432 of monomer A (a, b, c, d) and monomer B (e, f, g, h) and were calculated with the dark structure (including the two fatty-acid substrates and Wat1) as a phase model without refinement. The dark-state model is represented as sticks, with the C atoms of the protein in gray and those of the fatty-acid molecule in light green. |
![[Figure 4]](wa5138fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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