Thermus thermophilus cytochrome- c 552 : a new highly thermostable cytochrome- c structure obtained by MAD phasing 1 1Edited by K. Nagai

This publication has 58 references indexed in Scilit:

• Determinants of Enzyme Thermostability Observed in the Molecular Structure ofThermusaquaticusd-Glyceraldehyde-3-phosphate Dehydrogenase at 2.5 Å Resolution^,
  Biochemistry, 1996
• Dimeric 3‐Phosphoglycerate Kinases from Hyperthermophilic Archaea
  European Journal of Biochemistry, 1995
• The Crystal Structure of Holo-glyceraldehyde-3-phosphate Dehydrogenase from the Hyperthermophilic BacteriumThermotoga maritimaat 2.5 Å Resolution
  Journal of Molecular Biology, 1995
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• Proton NMR comparison of noncovalent and covalently cross-linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c
  Biochemistry, 1992
• Respiratory proteins from extremely thermophilic, aerobic bacteria
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1986
• Amino acid sequence of cytochrome c-552 from Thermusthermophilus HB8
  Biochemical and Biophysical Research Communications, 1985
• Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
  Biopolymers, 1983
• Ion-pairs in proteins
  Journal of Molecular Biology, 1983
• The independent distribution of amino acid near neighbor pairs into polypeptides
  Biochemical and Biophysical Research Communications, 1977