Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4H1P

Use of Europium for SAD Phasing at the Cu K alpha wavelength

Replaces:  4ENI
Summary for 4H1P
Entry DOI10.2210/pdb4h1p/pdb
Related1H87
DescriptorLysozyme C, EUROPIUM ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordshewl, lysozyme activity, catalytic activity, hydrolase
Biological sourceGallus gallus (bantam,chickens)
Total number of polymer chains1
Total formula weight15154.42
Authors
Vijayakumar, B.,Velmurugan, D. (deposition date: 2012-09-11, release date: 2012-10-24, Last modification date: 2024-11-20)
Primary citationVijayakumar, B.,Velmurugan, D.
Use of europium ions for SAD phasing of Lysozyme at the Cu Kalpha wavelength
Acta Crystallogr.,Sect.F, 69:20-24, 2013
Cited by
PubMed Abstract: Europium is shown to be a good anomalous scatterer in SAD phasing for solving the structure of biological macromolecules. The large value of the anomalous contribution of europium, f'' = 11.17 e(-), at the Cu Kα wavelength is an advantage in de novo phasing and automated model building. Tetragonal crystals of hen egg-white lysozyme (HEWL) incorporating europium(III) chloride (50 mM) were obtained which diffracted to a resolution of 2.3 Å at a wavelength of 1.54 Å (Cu Kα). The master data set (360° frames) was split and analyzed for anomalous signal-to-noise ratio, multiplicity, completeness, SAD phasing and automated building. The structure solution and model building of the split data sets were carried out using phenix.autosol and phenix.autobuild. The contributions of the Eu ions to SAD phasing using in-house data collection are discussed. This study revealed successful lysozyme phasing by SAD using laboratory-source data involving Eu ions, which are mainly coordinated by the side chains of Asn46, Asp52 and Asp101 together with some water molecules.
PubMed: 23295480
DOI: 10.1107/S1744309112047562
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

235183

PDB entries from 2025-04-23

PDB statisticsPDBj update infoContact PDBjnumon