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

Three types of protein–DNA complexes, AML1/Runx‐1/CBFα(Runt)–CBFβ–C/EBPβ(bZip)–DNA (CBFα‐β‐C/EBPβ‐DNA), AML1/Runx‐1/CBFα(Runt)–C/EBPβ(bZip)–DNA (CBFα‐C/EBPβ‐DNA) and AML1/Runx‐1/CBFα(Runt)–DNA (CBFα‐DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C2221, P2121...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-06, Vol.57 (6), p.850-853
Hauptverfasser: Tahirov, Tahir H., Inoue-Bungo, Taiko, Sasaki, Motoko, Shiina, Masaaki, Kimura, Kazumi, Sato, Ko, Kumasaka, Takashi, Yamamoto, Masaki, Kamiya, Nobuo, Ogata, Kazuhiro
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Sprache:eng
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Zusammenfassung:Three types of protein–DNA complexes, AML1/Runx‐1/CBFα(Runt)–CBFβ–C/EBPβ(bZip)–DNA (CBFα‐β‐C/EBPβ‐DNA), AML1/Runx‐1/CBFα(Runt)–C/EBPβ(bZip)–DNA (CBFα‐C/EBPβ‐DNA) and AML1/Runx‐1/CBFα(Runt)–DNA (CBFα‐DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C2221, P21212 and P212121, respectively. The resolutions of CBFα‐β‐C/EBPβ‐DNA and CBFα‐C/EBPβ‐DNA crystals were both 3 Å, while that of the CBFα‐DNA crystal was 2.65 Å. Complete data sets were collected for all of the native crystals, along with MAD and MIR data sets for CBFα‐β‐C/EBPβ‐DNA. The heavy‐atom site was determined using MAD data for a gold derivative of CBFα‐β‐C/EBPβ‐DNA.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444901003900