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5MVV

Crystal structure of Plasmodium falciparum actin I- gelsolin segment 1 -CdATP complex

Summary for 5MVV
Entry DOI10.2210/pdb5mvv/pdb
DescriptorActin-1, Gelsolin, ADENOSINE-5'-TRIPHOSPHATE, ... (7 entities in total)
Functional Keywordsexperimental phasing, cadmium, atp, actin, sad phasing, structural protein
Biological sourcePlasmodium falciparum (isolate 3D7)
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Total number of polymer chains2
Total formula weight57242.26
Authors
Panneerselvam, S.,Kumpula, E.-P.,Kursula, I.,Burkhardt, A.,Meents, A. (deposition date: 2017-01-17, release date: 2017-07-12, Last modification date: 2024-05-08)
Primary citationPanneerselvam, S.,Kumpula, E.P.,Kursula, I.,Burkhardt, A.,Meents, A.
Rapid cadmium SAD phasing at the standard wavelength (1 angstrom ).
Acta Crystallogr D Struct Biol, 73:581-590, 2017
Cited by
PubMed Abstract: Cadmium ions can be effectively used to promote crystal growth and for experimental phasing. Here, the use of cadmium ions as a suitable anomalous scatterer at the standard wavelength of 1 Å is demonstrated. The structures of three different proteins were determined using cadmium single-wavelength anomalous dispersion (SAD) phasing. Owing to the strong anomalous signal, the structure of lysozyme could be automatically phased and built using a very low anomalous multiplicity (1.1) and low-completeness (77%) data set. Additionally, it is shown that cadmium ions can easily substitute divalent ions in ATP-divalent cation complexes. This property could be generally applied for phasing experiments of a wide range of nucleotide-binding proteins. Improvements in crystal growth and quality, good anomalous signal at standard wavelengths (i.e. no need to change photon energy) and rapid phasing and refinement using a single data set are benefits that should allow cadmium ions to be widely used for experimental phasing.
PubMed: 28695858
DOI: 10.1107/S2059798317006970
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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