2JHO
Cyanomet Sperm Whale Myoglobin at 1.4A resolution
Summary for 2JHO
| Entry DOI | 10.2210/pdb2jho/pdb |
| Related | 101M 102M 103M 104M 105M 106M 107M 108M 109M 110M 111M 112M 1A6G 1A6K 1A6M 1A6N 1ABS 1AJG 1AJH 1BVC 1BVD 1BZ6 1BZP 1BZR 1CH1 1CH2 1CH3 1CH5 1CH7 1CH9 1CIK 1CIO 1CO8 1CO9 1CP0 1CP5 1CPW 1CQ2 1DO1 1DO3 1DO4 1DO7 1DTI 1DTM 1DUK 1DUO 1DXC 1DXD 1EBC 1F63 1F65 1F6H 1FCS 1H1X 1HJT 1IOP 1IRC 1J3F 1J52 1JDO 1JP6 1JP8 1JP9 1JPB 1JW8 1L2K 1LTW 1LUE 1MBC 1MBD 1MBI 1MBN 1MBO 1MCY 1MGN 1MLF 1MLG 1MLH 1MLJ 1MLK 1MLL 1MLM 1MLN 1MLO 1MLQ 1MLR 1MLS 1MLU 1MOA 1MOB 1MOC 1MOD 1MTI 1MTJ 1MTK 1MYF 1MYM 1MYZ 1MZ0 1N9F 1N9H 1N9I 1N9X 1NAZ 1O16 1OBM 1OFJ 1OFK 1SPE 1SWM 1TES 1U7R 1U7S 1UFJ 1UFP 1VXA 1VXB 1VXC 1VXD 1VXE 1VXF 1VXG 1VXH 1WVP 1YOG 1YOH 1YOI 2BLH 2BLI 2BLJ 2BW9 2BWH 2CDJ 2CDK 2CDL 2CMM 2D6C 2EVP 2G0R 2G0S 2G0V 2G0X 2G0Z 2G10 2G11 2G12 2G14 2MB5 2MBW 2MGA 2MGB 2MGC 2MGD 2MGE 2MGF 2MGG 2MGH 2MGI 2MGJ 2MGK 2MGL 2MGM 2MYA 2MYB 2MYC 2MYD 2MYE 2SPL 2SPM 2SPN 2SPO 4MBN 5MBN |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (6 entities in total) |
| Functional Keywords | oxygen transport, heme, iron, transport, metal-binding, muscle protein |
| Biological source | Physeter catodon (Sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18235.53 |
| Authors | Arcovito, A.,Benfatto, M.,Cianci, M.,Hasnain, S.S.,Nienhaus, K.,Nienhaus, G.U.,Savino, C.,Strange, R.W.,Vallone, B.,Della Longa, S. (deposition date: 2007-02-23, release date: 2007-04-03, Last modification date: 2023-12-13) |
| Primary citation | Arcovito, A.,Benfatto, M.,Cianci, M.,Hasnain, S.S.,Nienhaus, K.,Nienhaus, G.U.,Savino, C.,Strange, R.W.,Vallone, B.,Della Longa, S. X-ray structure analysis of a metalloprotein with enhanced active-site resolution using in situ x-ray absorption near edge structure spectroscopy. Proc. Natl. Acad. Sci. U.S.A., 104:6211-6216, 2007 Cited by PubMed Abstract: X-ray absorption spectroscopy is exquisitely sensitive to the coordination geometry of an absorbing atom and therefore allows bond distances and angles of the surrounding atomic cluster to be measured with atomic resolution. By contrast, the accuracy and resolution of metalloprotein active sites obtainable from x-ray crystallography are often insufficient to analyze the electronic properties of the metals that are essential for their biological functions. Here, we demonstrate that the combination of both methods on the same metalloprotein single crystal yields a structural model of the protein with exceptional active-site resolution. To this end, we have collected an x-ray diffraction data set to 1.4-A resolution and Fe K-edge polarized x-ray absorption near edge structure (XANES) spectra on the same cyanomet sperm whale myoglobin crystal. The XANES spectra were quantitatively analyzed by using a method based on the multiple scattering approach, which yielded Fe-heme structural parameters with +/-(0.02-0.07)-A accuracy on the atomic distances and +/-7 degrees on the Fe-CN angle. These XANES-derived parameters were subsequently used as restraints in the crystal structure refinement. By combining XANES and x-ray diffraction, we have obtained an cyanomet sperm whale myoglobin structural model with a higher precision of the bond lengths and angles at the active site than would have been possible with crystallographic analysis alone. PubMed: 17404234DOI: 10.1073/pnas.0608411104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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