| Autor: |
Resch M; Lehrstuhl für Biotechnik, Department of Biology, Friederich-Alexander University Erlangen-Nuremberg, Erlangen, Germany., Roth HM, Kottmair M, Sevvana M, Bertram R, Titgemeyer F, Muller YA |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2009 Apr 01; Vol. 65 (Pt 4), pp. 410-4. Date of Electronic Publication: 2009 Mar 26. |
| DOI: |
10.1107/S1744309109008628 |
| Abstrakt: |
The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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