Crystallization and preliminary X-ray analyses of quaternary, ternary and binary protein–DNA complexes with involvement of AML1/Runx-1/CBFα Runt domain, CBFβ and the C/EBPβ bZip region
| Autor: | Kazuhiro Ogata, Nobuo Kamiya, Ko Sato, Masaki Yamamoto, Kazumi Kimura, Takashi Kumasaka, Motoko Sasaki, Masaaki Shiina, Tahir H. Tahirov, Taiko Inoue-Bungo |
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| Rok vydání: | 2001 |
| Předmět: |
Core Binding Factor alpha Subunits
Protein Conformation Crystallography X-Ray law.invention Mice Protein structure Structural Biology law Proto-Oncogene Proteins Animals Crystallization Chemistry CCAAT-Enhancer-Binding Protein-beta Runt X-ray Space group DNA General Medicine Recombinant Proteins Neoplasm Proteins DNA-Binding Proteins Crystallography Core Binding Factor Alpha 2 Subunit Nucleic Acid Conformation Orthorhombic crystal system Peptides Ternary operation Transcription Factors |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 57:850-853 |
| ISSN: | 0907-4449 |
| Popis: | Three types of protein-DNA complexes, AML1/Runx-1/CBFalpha(Runt)-CBFbeta-C/EBPbeta(bZip)-DNA (CBFalpha-beta-C/EBPbeta-DNA), AML1/Runx-1/CBFalpha(Runt)-C/EBPbeta(bZip)-DNA (CBFalpha-C/EBPbeta-DNA) and AML1/Runx-1/CBFalpha(Runt)-DNA (CBFalpha-DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C222(1), P2(1)2(1)2 and P2(1)2(1)2(1), respectively. The resolutions of CBFalpha-beta-C/EBPbeta-DNA and CBFalpha-C/EBPbeta-DNA crystals were both 3 A, while that of the CBFalpha-DNA crystal was 2.65 A. Complete data sets were collected for all of the native crystals, along with MAD and MIR data sets for CBFalpha-beta-C/EBPbeta-DNA. The heavy-atom site was determined using MAD data for a gold derivative of CBFalpha-beta-C/EBPbeta-DNA. |
| Databáze: | OpenAIRE |
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