Publikation: Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2
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2010
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Acta Crystallographica Section F : Structural Biology and Crystallization Communications. International Union of Crystallography (IUCr). 2010, 66(Pt 9), pp. 1032-1036. ISSN 2053-230X. eISSN 1744-3091. Available under: doi: 10.1107/S1744309110030691
Zusammenfassung
Human S100A2 is an EF-hand protein and acts as a major tumour suppressor, binding and activating p53 in a Ca2+-dependent manner. Ca2+-bound S100A2 was crystallized and its structure was determined based on the anomalous scattering provided by six S atoms from methionine residues and four calcium ions present in the asymmetric unit. Although the diffraction data were recorded at a wavelength of 0.90 Å, which is usually not assumed to be suitable for calcium/sulfur SAD, the anomalous signal was satisfactory. A nine-atom substructure was determined at 1.8 Å resolution using SHELXD, and SHELXE was used for density modification and phase extension to 1.3 Å resolution. The electron-density map obtained was well interpretable and could be used for automated model building by ARP/wARP.
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KOCH, Michael, Joachim DIEZ, Armin WAGNER, Günter FRITZ, 2010. Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2. In: Acta Crystallographica Section F : Structural Biology and Crystallization Communications. International Union of Crystallography (IUCr). 2010, 66(Pt 9), pp. 1032-1036. ISSN 2053-230X. eISSN 1744-3091. Available under: doi: 10.1107/S1744309110030691BibTex
@article{Koch2010-09-01Cryst-52710,
year={2010},
doi={10.1107/S1744309110030691},
title={Crystallization and calcium/sulfur SAD phasing of the human EF-hand protein S100A2},
number={Pt 9},
volume={66},
issn={2053-230X},
journal={Acta Crystallographica Section F : Structural Biology and Crystallization Communications},
pages={1032--1036},
author={Koch, Michael and Diez, Joachim and Wagner, Armin and Fritz, Günter}
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<dcterms:abstract xml:lang="eng">Human S100A2 is an EF-hand protein and acts as a major tumour suppressor, binding and activating p53 in a Ca<sup>2+</sup>-dependent manner. Ca<sup>2+</sup>-bound S100A2 was crystallized and its structure was determined based on the anomalous scattering provided by six S atoms from methionine residues and four calcium ions present in the asymmetric unit. Although the diffraction data were recorded at a wavelength of 0.90 Å, which is usually not assumed to be suitable for calcium/sulfur SAD, the anomalous signal was satisfactory. A nine-atom substructure was determined at 1.8 Å resolution using SHELXD, and SHELXE was used for density modification and phase extension to 1.3 Å resolution. The electron-density map obtained was well interpretable and could be used for automated model building by ARP/wARP.</dcterms:abstract>
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