1h87
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==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, ... | + | 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== | ==About this Structure== | ||
| - | 1H87 is a | + | 1H87 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with CL, DO3 and GD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Structure known Active Site: LG1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H87 OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: o-glycosyl hydrolase]] | [[Category: o-glycosyl hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:56:21 2007'' |
Revision as of 11:51, 5 November 2007
|
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 with CL, DO3 and GD as ligands. Active as Lysozyme, with EC number 3.2.1.17 Structure known Active Site: LG1. 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 Nov 5 13:56:21 2007
Categories: Gallus gallus | Lysozyme | Single protein | Chantalat, L. | Girard, E. | Kahn, R. | Vicat, J. | CL | DO3 | GD | Gadolinium derivative | O-glycosyl hydrolase
