Crystallization and preliminary X-ray characterization of the Methanothermus fervidus histones HMfA and HMfB

Proteins: Structure, Function and Genetics

Volumn 24, Issue 2, 1996, Pages 269-271

  Decanniere, Klaas ^a   Sandman, Kathleen ^b   Reeve, John N ^b   Heinemann, Udo ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

anomalous dispersion; Archaea; histone fold; hyperthermophiles; X ray diffraction

Indexed keywords

BACTERIAL PROTEIN; HISTONE; SELENOMETHIONINE;

ARTICLE; AUXOTROPHIC MUTANT; CRYSTALLIZATION; ESCHERICHIA COLI; METHANOBACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STRUCTURE; X RAY DIFFRACTION;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; EURYARCHAEOTA; HISTONES; RECOMBINANT PROTEINS;

EID: 0029670127     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199602)24:2<269::AID-PROT16>3.0.CO;2-L     Document Type: Article

References (19)

1. Sandman, K., Krzycki, J.A., Dobrinski, B., Lurz, R., Reeve, J.N. HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon Methanothermus fervidus, is most closely related to histones. Proc. Natl. Acad. Sci. USA 87:5788-5791, 1990.
2. Musgrave, D.R., Sandman, K.M., Reeve, J.N. DNA binding by the archaeal histone HMf results in positive super-coiling. Proc. Natl. Acad. Sci. USA 88:10397-10401, 1991.
3. Howard, M.T., Sandman, K., Reeve, J.N., Griffith, J.D. HMf, a histone-related protein from the hyperthermophilic archaeon Methanothermus fervidus, binds preferentially to DNA containing phased tracts of adenines. J. Bacteriol. 174:7864-7867, 1992.
4. Stroup, D., Reeve, J.N. Histone HMf from the hyperthermophilic archaeon Methanothermus fervidus binds to DNA in vitro using physiological conditions. FEMS Microbiol. Letters 91:271-276, 1992.
5. Grayling, H.A., Becktel, W.J., Reeve, J.N. Structure and stability of histone HMf from the hyperthermophilic archaeon Methanothermus fervidus. Biochemistry 34:8441-8448, 1995.
6. Wells, D., McBride, C. A comprehensive compilation and alignment of histones and histone genes. Nucleic Acids Res. 17(suppl.):r311-r346, 1989.
7. Arents, G., Burlingame, R.W., Wang, B.-C., Love, W.E., Moudrianakis, E N. The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. USA 88: 10148-10152, 1991.
8. Arents, G., Moudrianakis, E.N. Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl. Acad. Sci. USA 90:10489-10493, 1993.
9. Sandman, K., Grayling, R.A., Dobrinski, B., Lurz, R., Reeve, J.N. Growth phase dependent synthesis of histones in the archaeon Methanothermus fervidus. Proc. Natl. Acad. Sci. USA 91:12624-12628, 1994.
10. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K. Short Protocols in Molecular Biology. New York: John Wiley & Sons, 1989.
11. Sandman, K., Grayling, R.A , Reeve, J.N. Improved N-terminal processing of recombinant proteins synthesized in Escherichia coli. Bio/Technology 13:504-506, 1995.
12. Kuo, C.-F., McRee, D.E., Cunningham, R.P., Tainer, J.A. Purification, crystallization and space group determination of DNA repair enzyme exonuclease III from E. coli. J. Mol. Biol. 229:239-242, 1993.
13. Jancarik, J., Kim, S.-H. Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24:409-411, 1991.
14. Cudney, B., Patel, S., Weisgraber, K., Newhouse, Y., McPherson, A. Screening and optimization strategies for macromolecular crystal growth. Acta Crystallogr. D50: 414-423, 1994.
15. Otwinowski, Z. DENZO: An Oscillation Data Processing Program for Macromolecular Crystallography New Haven, CT: Yale University, 1993.
16. Collaborative Computational Project, Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50:760-763, 1994.
17. Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol. 33:491-497, 1968.
18. Hendrickson, W.A., Horton, J.R., LeMaster, D.M. Selenomethionyl proteins produced for analysis by multiwave-length anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J. 9:1665-1672, 1990.
19. Glover, I.D., Denny, R.C., Nguti, N.D., McSweeney, S.M., Kinder, S.H., Thompson, A.W., Dodson, E.J., Wilkinson, A.J., Tame, J.R.H. Structure determination of OppA at 2.3 A resolution using multiple-wavelength anomalous dispersion methods. Acta Crystallogr. D51:39-47, 1995.