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@ARTICLE{Choe:26893,
      author       = {Choe, B. J. and Jeong, D.-G. and Park, K. S. and
                      Schlesinger, R. and Labahn, J. and Hofmann, K. P. and
                      Büldt, G.},
      title        = {{P}reliminary {X}-ray characterization of the ribonuclease
                      {P} ({C}5 protein) from {E}scherichia coli : expression,
                      crystallization and cryoconditions},
      journal      = {Acta crystallographica / D},
      volume       = {59},
      issn         = {0907-4449},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {PreJuSER-26893},
      pages        = {350 - 352},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The gene for Escherichia coli ribonuclease P (RNase P)
                      protein (also known as C5 protein) and its mutant C5-C113A
                      have been expressed as GST fusion proteins in E. coli at a
                      high level. After cleavage of the fusion protein, highly
                      purified functional C5 protein is obtained that can be
                      crystallized with 2.5-2.6 M
                      (NH(4))(2)HPO(4)/(NH(4))H(2)PO(4) pH 7.0 at room
                      temperature. These crystals are suitable for X-ray analysis,
                      belong to the space group P3(1)21 or P3(2)21 (unit-cell
                      parameters a = b = 66.67, c = 142.09 A) and diffract to 2.9
                      A at 100 K using sorbitol and glycerol as cryoprotectants.
                      For three molecules in the asymmetric unit a V(M) of 2.17
                      A(3) Da(-1) was calculated.},
      keywords     = {Amino Acid Substitution / Cryoprotective Agents: chemistry
                      / Crystallization / Crystallography, X-Ray /
                      Endoribonucleases: chemistry / Endoribonucleases: genetics /
                      Endoribonucleases: metabolism / Escherichia coli: enzymology
                      / Escherichia coli Proteins / Glutathione Transferase:
                      genetics / Glycerol: chemistry / RNA, Catalytic: chemistry /
                      RNA, Catalytic: genetics / RNA, Catalytic: metabolism /
                      Recombinant Fusion Proteins: biosynthesis / Recombinant
                      Fusion Proteins: genetics / Ribonuclease P /
                      Ribonucleoproteins: chemistry / Ribonucleoproteins: genetics
                      / Ribonucleoproteins: metabolism / Sorbitol: chemistry /
                      Cryoprotective Agents (NLM Chemicals) / Escherichia coli
                      Proteins (NLM Chemicals) / RNA, Catalytic (NLM Chemicals) /
                      Recombinant Fusion Proteins (NLM Chemicals) /
                      Ribonucleoproteins (NLM Chemicals) / Sorbitol (NLM
                      Chemicals) / Glycerol (NLM Chemicals) / Glutathione
                      Transferase (NLM Chemicals) / Endoribonucleases (NLM
                      Chemicals) / Ribonuclease P (NLM Chemicals) / ribonuclease
                      P, E coli (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemical Research Methods / Biochemistry $\&$ Molecular
                      Biology / Biophysics / Crystallography},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12554950},
      UT           = {WOS:000180641900020},
      doi          = {10.1107/S0907444902020784},
      url          = {https://juser.fz-juelich.de/record/26893},
}