5AI2

Anomalous Neutron phased crystal structure of 113Cd-substituted Perdeuterated Pyrococcus furiosus rubredoxin to 1.75A resolution at 295K

Summary for 5AI2

• Entry DOI: 10.2210/pdb5ai2/pdb
• Related: 5AI3
• Descriptor: RUBREDOXIN, CADMIUM ION, deuterium(1+), ... (4 entities in total)
• Functional Keywords: electron transport, neutron anomalous phasing, perdeuterated, pyrococcus furiosus, rubredoxin, cadmium
• Biological source: PYROCOCCUS FURIOSUS
• Total number of polymer chains: 1
• Total formula weight: 6150.18

Authors

Cuypers, M.G.,Mossou, E.,Mason, S.A. (deposition date: 2015-02-11, release date: 2016-03-02, Last modification date: 2024-05-08)

Primary citation

Cuypers, M.G.,Mason, S.A.,Mossou, E.,Haertlein, M.,Forsyth, V.T.,Mitchell, E.P.
Macromolecular Structure Phasing by Neutron Anomalous Diffraction.
Sci.Rep., 6:31487-, 2016

PubMed Abstract: In this report we show for the first time that neutron anomalous dispersion can be used in a practical manner to determine experimental phases of a protein crystal structure, providing a new tool for structural biologists. The approach is demonstrated through the use of a state-of-the-art monochromatic neutron diffractometer at the Institut Laue-Langevin (ILL) in combination with crystals of perdeuterated protein that minimise the level of hydrogen incoherent scattering and enhance the visibility of the anomalous signal. The protein used was rubredoxin in which cadmium replaced the iron at the iron-sulphur site. While this study was carried out using a steady-state neutron beam source, the results will be of major interest for capabilities at existing and emerging spallation neutron sources where time-of-flight instruments provide inherent energy discrimination. In particular this capability may be expected to offer unique opportunities to a rapidly developing structural biology community where there is increasing interest in the identification of protonation states, protein/water interactions and protein-ligand interactions - all of which are of central importance to a wide range of fundamental and applied areas in the biosciences.

PubMed: 27511806
DOI: 10.1038/SREP31487

Experimental method

NEUTRON DIFFRACTION (1.75 Å)