1h87
From Proteopedia
GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG-WHITE LYSOZYME AT 1.7 A RESOLUTION
Overview
A neutral gadolinium complex, Gd-HPDO3A, is shown to be a good candidate to use to obtain heavy-atom derivatives and solve macromolecular structures using anomalous dispersion. Tetragonal crystals of a gadolinium derivative of hen egg-white lysozyme were obtained by co-crystallization using different concentrations of the complex. Diffraction data from three derivative crystals (100, 50 and 10 mM) were collected to a resolution of 1.7 A using Cu Kalpha radiation from a rotating anode. Two strong binding sites of the gadolinium complex to the protein were located from the gadolinium anomalous signal in both the 100 and 50 mM derivatives. A single site is occupied in the 10 mM derivative. Phasing using the anomalous signal at a single wavelength (SAD method) leads to an electron-density map of high quality. The structure of the 100 mM derivative has been refined. Two molecules of the gadolinium complex are close together. Both molecules are located close to tryptophan residues. Four chloride ions were found. The exceptional quality of the SAD electron-density map, only enhanced by solvent flattening, suggests that single-wavelength anomalous scattering with the Gd-HPDO3A complex may be sufficient to solve protein structures of high molecular weight by synchrotron-radiation experiments, if not by laboratory experiments.
About this Structure
1H87 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Gd-HPDO3A, a complex to obtain high-phasing-power heavy-atom derivatives for SAD and MAD experiments: results with tetragonal hen egg-white lysozyme., Girard E, Chantalat L, Vicat J, Kahn R, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):1-9. Epub 2001 Dec, 21. PMID:11752774 Page seeded by OCA on Fri May 2 18:33:32 2008
