Generalized X-ray and neutron crystallographic analysis: more accurate and complete structures for biological macromolecules

By Paul D. Adams, M. Mustyakimov, Pavel V. Afonine, P. Langan. 2009

122 citations recorded by the source corpus.

X-ray and neutron crystallographic data have been combined in a joint structure-refinement procedure that has been developed using recent advances in modern computational methodologies, including cross-validated maximum-likelihood target functions with gradient-based optimization and simulated annealing.

Subfields: Materials Chemistry, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

In Molecular Biology

Citations in the corpus

Towards automated crystallographic structure refinement with phenix.refine (2012, methodology): “When joint refinement is performed using both X-ray and neutron data (Coppens et al., 1981; Wlodawer & Hendrickson, 1981, 1982; Adams et al., 2009; Afonine, Mustyakimov et al., 2010), it is important to ensure that the cross-validation reflections are consistent between data sets.”
Recent developments in phasing and structure refinement for macromolecular crystallography (2009, background): “Recent work has demonstrated that the joint (simultaneous) refinement of a single model against X-ray and neutron data leads to an improved model, as judged by both X-ray and neutron Rfactors [50 ].”
Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition (2018, methodology): “…low signal to noise and the increased number of parameters, the concept of joint X-ray and neutron refinement (hereafter referred to as joint XN refinement) was introduced (Coppens, 1967; Orpen et al., 1978; Wlodawer, 1980; Wlodawer & Hendrickson, 1982; Adams et al., 2009; Afonine et al., 2010).”
Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP γ-Phosphate* (2015, background): “The structure pushes the limits of neutron crystallography both in terms of its high resolution, allowing refinement in the absence of combined x-ray data (46, 47), and in the fact that the crystal form has a relatively large unit cell (Table 1).”
Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase. (2013, methodology): “Joint neutron and X-ray structure refinement is in progress using both a modified version of CNS for neutrons (nCNS) and phenix.refine (Adams et al., 2009; Afonine et al., 2010).”