Neutron diffraction studies towards deciphering the protonation state of catalytic residues in the bacterial KDN9P phosphatase.

By Tyrel L Bryan, Javier M. González, J. Bacik, N. Denunzio, Clifford J. Unkefer, T. Schrader, A. Ostermann, D. Dunaway-Mariano, S. Z. Fisher. 2013

7 citations recorded by the source corpus.

Subfields: Endocrinology, Diabetes and Metabolism, 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 Endocrinology, Diabetes and Metabolism

1. T. Croll

In Materials Chemistry

1. Paul D. Adams
2. Pavel V. Afonine
3. Randy J. Read
4. T. C. Terwilliger
5. Nigel W. Moriarty
6. T. Croll
7. A. McCoy
8. Jane S. Richardson

In Molecular Biology

1. Paul D. Adams
2. Pavel V. Afonine
3. Randy J. Read
4. T. C. Terwilliger
5. Nigel W. Moriarty
6. T. Croll
7. A. McCoy
8. Jane S. Richardson

Citations in the corpus

• Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix (2019, background): “It is therefore possible to locate H (or D) atoms and to deduce their protonation states; this knowledge helps in understanding catalytic mechanisms and ligand binding (Yamaguchi et al., 2009; Bryan et al., 2013; Knihtila et al., 2015).”
• Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition (2018, background): “…al., 2003; Weber et al., 2013; Haupt et al., 2014; Casadei et al., 2014; Howard et al., 2016), neutron diffraction is able to provide valuable information for the understanding of catalytic mechanisms and ligand binding (Yamaguchi et al., 2009; Bryan et al., 2013; Knihtila et al., 2015).”