X-ray structure determination at low resolution

By A. Brunger, B. Delabarre, J. Davies, William I. Weis. 2009

53 citations recorded by the source corpus.

Refinement is meaningful even at 4 Å or lower, but with present methodologies it should start from high-resolution crystal structures whenever possible.

Subfields: Materials Chemistry, Molecular Biology

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In Materials Chemistry

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Citations in the corpus

FEM: feature-enhanced map (2014, methodology): “This technique has been shown to be useful in improving the interpretability of lowresolution maps (see Brunger et al., 2009 and references therein).”
Current approaches for the fitting and refinement of atomic models into cryo-EM maps using CCP-EM (2018, methodology): “Map sharpening has been used to counter over-blurred maps, resulting in features in the map being revealed (Brunger et al., 2009; Nicholls et al., 2012), noting that other approaches towards map modification have been employed with a similar objective both in the context of MX (Afonine et al.,…”
Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain (2016, background): “DISCUSSION iMDFF and the IR Ectodomain There is a need to increase the speed and fidelity of crystallographic model building at low resolution (Brünger et al., 2009).”
Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta (2016, background): “Furthermore, such model building and refinement is challenging and error prone ( DeLaBarre and Brunger, 2006 ; Brunger et al., 2009 ).”
Recent developments in phasing and structure refinement for macromolecular crystallography (2009, unknown): “7 Å resolution [47,48 ].”