1h87
From Proteopedia
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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, ... [(full description)]
About this Structure
1H87 is a [Single protein] structure of sequence from [[1]] with CL, DO3 and GD as [ligands]. Active as [[2]], with EC number [3.2.1.17]. 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 Mon Oct 29 19:11:23 2007
Categories: Single protein | Chantalat, L. | Girard, E. | Kahn, R. | Vicat, J. | CL | DO3 | GD | Gadolinium derivative | Lysozyme | O-glycosyl hydrolase