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![[Figure 2]](nw5141fig2mag.jpg)
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Figure 2
Genuine deformation density in the rubredoxin structure at 0.43 Å resolution. Depicted are 2mFo − DFc maps contoured at 2.0 e Å−3 in (a), (f), (k) and (p), mFo − DFc,IAM maps contoured at ±0.55 e Å−3 in (b), (g), (l) and (q), deformation density (Fc,TAAM − Fc,IAM) maps contoured at ±0.25 e Å−3 in (c), (h), (m) and (r), and mFo − DFc,TAAM maps contoured at ±0.55 e Å−3 in (d), (i), (n) and (s), as well as mFo − DFc,IAM (hydrogen-omit) maps contoured at ±0.8 e Å−3 in (e), (j), (o) and (t). In (a)–(e) the Fe–S4 site is shown, in (f)–(j) Tyr11, in (k)–(o) the Trp37-Val38 dipeptide and finally in (p)–(t) Gly43. Note that the majority of positive difference density visible in mFo − DFc,IAM maps resembles features in the deformation map, and these features are not present in the mFo − DFc,TAAM maps, providing evidence that mFo − DFc,IAM map density features indeed represent deformation density. The Fe–S4 site was refined with IAM scattering factors, as no aspherical descriptions exist in the MATTS databank. All maps were computed by rejecting 383 reflections, which corresponds to a log-likelihood level of −4. |
![[Figure 2]](nw5141fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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