1H87
Gadolinium derivative of tetragonal Hen Egg-White Lysozyme at 1.7 A resolution
Summary for 1H87
| Entry DOI | 10.2210/pdb1h87/pdb |
| Related | 132L 193L 194L 1A2Y 1AKI 1AT5 1AT6 1AZF 1B0D 1B2K 1BGI 1BHZ 1BVK 1BVX 1BWH 1BWI 1BWJ 1C08 1C10 1DPW 1DPX 1DQJ 1E8L 1F0W 1F10 1F3J 1FDL 1FLQ 1FLU 1FLW 1FLY 1FN5 1G7H 1G7I 1G7J 1G7L 1G7M 1HEL 1HEM 1HEN 1HEO 1HEP 1HEQ 1HER 1HEW 1HF4 1HSW 1HSX 1JPO 1KIP 1KIQ 1KIR 1KXW 1KXX 1KXY 1LCN 1LKR 1LKS 1LMA 1LPI 1LSA 1LSB 1LSC 1LSD 1LSE 1LSF 1LSG 1LSM 1LSN 1LSY 1LSZ 1LYO 1LYS 1LYZ 1LZ8 1LZA 1LZB 1LZC 1LZD 1LZE 1LZG 1LZH 1LZN 1LZT 1MEL 1MLC 1QTK 1RCM 1RFP 1UCO 1UIA 1UIB 1UIC 1UID 1UIE 1UIF 1UIG 1UIH 1XEI 1XEJ 1XEK 2HFM 2IFF 2LYM 2LYO 2LYZ 2LZH 2LZT 3HFL 3HFM 3LYM 3LYO 3LYT 3LYZ 3LZT 4LYM 4LYO 4LYT 4LYZ 4LZT 5LYM 5LYT 5LYZ 6LYT 6LYZ 7LYZ 8LYZ |
| Descriptor | LYSOZYME C, 10-((2R)-2-HYDROXYPROPYL)-1,4,7,10-TETRAAZACYCLODODECANE 1,4,7-TRIACETIC ACID, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, gadolinium derivative, lysozyme, o-glycosyl hydrolase |
| Biological source | GALLUS GALLUS (CHICKEN) |
| Total number of polymer chains | 1 |
| Total formula weight | 15596.39 |
| Authors | Girard, E.,Chantalat, L.,Vicat, J.,Kahn, R. (deposition date: 2001-01-25, release date: 2002-01-15, Last modification date: 2024-11-13) |
| Primary citation | Girard, E.,Chantalat, L.,Vicat, J.,Kahn, R. Gd-Hp-Do3A, a Complex to Obtain High-Phasing-Power Heavy Atom Derivatives for Sad and MAD Experiments. Results with Tetragonal Hen Egg-White Lysozyme Acta Crystallogr.,Sect.D, 58:1-, 2001 Cited by PubMed Abstract: 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. PubMed: 11752774DOI: 10.1107/S0907444901016444 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.72 Å) |
Structure validation
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