Crystal structure of PriB, a component of the Escherichia coli replication restart primosome.

[1]  J. Keck,et al.  Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[2]  Tom Alber,et al.  Automated protein crystal structure determination using ELVES. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[3]  M. Cox,et al.  The single-stranded DNA-binding protein of Deinococcus radiodurans , 2004, BMC Microbiology.

[4]  Deborah S Wuttke,et al.  Nucleic acid recognition by OB-fold proteins. , 2003, Annual review of biophysics and biomolecular structure.

[5]  J. Thornton,et al.  Diversity of protein–protein interactions , 2003, The EMBO journal.

[6]  E. Koonin,et al.  Gene Duplication with Displacement and Rearrangement: Origin of the Bacterial Replication Protein PriB from the Single-Stranded DNA-Binding Protein Ssb , 2003, Journal of Molecular Microbiology and Biotechnology.

[7]  E. Snell,et al.  The development and application of a method to quantify the quality of cryoprotectant solutions using standard area-detector X-ray images , 2002 .

[8]  G. Waksman,et al.  Structure of the DNA binding domain of E. coli SSB bound to ssDNA , 2000, Nature Structural Biology.

[9]  Myron F. Goodman,et al.  The importance of repairing stalled replication forks , 2000, Nature.

[10]  S. Sandler,et al.  Role of PriA in Replication Fork Reactivation inEscherichia coli , 2000, Journal of bacteriology.

[11]  S. Sandler,et al.  dnaC mutations suppress defects in DNA replication‐ and recombination‐associated functions in priB and priC double mutants in Escherichia coli K‐12 , 1999, Molecular microbiology.

[12]  J. Liu,et al.  PriA-directed Assembly of a Primosome on D Loop DNA* , 1999, The Journal of Biological Chemistry.

[13]  A. Edwards,et al.  The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single‐stranded DNA binding , 1999, The EMBO journal.

[14]  Thomas C. Terwilliger,et al.  Automated MAD and MIR structure solution , 1999, Acta crystallographica. Section D, Biological crystallography.

[15]  D. Smith,et al.  The role of the 6 lysines and the terminal amine of escherichia coli single‐strand binding protein in its binding of single‐stranded DNA , 1998, Protein science : a publication of the Protein Society.

[16]  Cheng Yang,et al.  Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution , 1997, Nature Structural Biology.

[17]  J. Liu,et al.  The ordered assembly of the phiX174-type primosome. III. PriB facilitates complex formation between PriA and DnaT. , 1996, The Journal of biological chemistry.

[18]  K. Marians,et al.  The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes. , 1996, The Journal of biological chemistry.

[19]  A. Kornberg,et al.  Assembly of the primosome of DNA replication in Escherichia coli. , 1993, The Journal of biological chemistry.

[20]  A. Murzin.  OB(oligonucleotide/oligosaccharide binding)‐fold: common structural and functional solution for non‐homologous sequences. , 1993, The EMBO journal.

[21]  K. Sharp,et al.  Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.

[22]  K. Zavitz,et al.  The priB and priC replication proteins of Escherichia coli. Genes, DNA sequence, overexpression, and purification. , 1991, The Journal of biological chemistry.

[23]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[24]  Wolfgang Kabsch,et al.  Evaluation of Single-Crystal X-ray Diffraction Data from a Position-Sensitive Detector , 1988 .

[25]  A. Kornberg,et al.  Replication initiated at the origin (oriC) of the E. coli chromosome reconstituted with purified enzymes , 1984, Cell.

[26]  A. Kornberg,et al.  Protein n, a primosomal DNA replication protein of Escherichia coli. Purification and characterization. , 1982, The Journal of biological chemistry.

[27]  R. Schekman,et al.  Ten proteins required for conversion of phiX174 single-stranded DNA to duplex form in vitro. Resolution and reconstitution. , 1975, The Journal of biological chemistry.

[28]  J. Hurwitz,et al.  Conversion of phiX174 viral DNA to double-stranded form by purified Escherichia coli proteins. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[29]  W. Delano.  The PyMOL Molecular Graphics System , 2002 .

[30]  G N Murshudov,et al.  Use of TLS parameters to model anisotropic displacements in macromolecular refinement. , 2001, Acta crystallographica. Section D, Biological crystallography.

[31]  V S Lamzin,et al.  Automated refinement of protein models. , 1993, Acta crystallographica. Section D, Biological crystallography.