Chapter 1.2. Historical background

References

Adams, M. J., Blundell, T. L., Dodson, E. J., Dodson, G. G., Vijayan, M., Baker, E. N., Harding, M. M., Hodgkin, D. C., Rimmer, B. & Sheat, S. (1969). Structure of rhombohedral 2 zinc insulin crystals. Nature (London), 224, 491–495.Google Scholar
Adams, M. J., Ford, G. C., Koekoek, R., Lentz, P. J. Jr, McPherson, A. Jr, Rossmann, M. G., Smiley, I. E., Schevitz, R. W. & Wonacott, A. J. (1970). Structure of lactate dehydrogenase at 2.8 Å resolution. Nature (London), 227, 1098–1103.Google Scholar
Astbury, W. T. (1933). Fundamentals of fiber structure. Oxford University Press.Google Scholar
Astbury, W. T., Mauguin, C., Hermann, C., Niggli, P., Brandenberger, E. & Lonsdale-Yardley, K. (1935). Space groups. In Internationale Tabellen zur Bestimmung von Kristallstrukturen, edited by C. Hermann, Vol. 1, pp. 84–87. Berlin: Begrüder Borntraeger.Google Scholar
Beevers, C. A. & Lipson, H. (1934). A rapid method for the summation of a two-dimensional Fourier series. Philos. Mag. 17, 855–859.Google Scholar
Bernal, J. D. (1933). Comments. Chem. Ind. 52, 288.Google Scholar
Bernal, J. D. & Crowfoot, D. (1934). X-ray photographs of crystalline pepsin. Nature (London), 133, 794–795.Google Scholar
Bernal, J. D. & Fankuchen, I. (1941). X-ray and crystallographic studies of plant virus preparations. J. Gen. Physiol. 25, 111–165.Google Scholar
Bernal, J. D., Fankuchen, I. & Perutz, M. (1938). An X-ray study of chymotrypsin and haemoglobin. Nature (London), 141, 523–524.Google Scholar
Bijvoet, J. M. (1949). K. Ned. Akad. Wet. 52, 313.Google Scholar
Bijvoet, J. M., Peerdeman, A. F. & van Bommel, A. J. (1951). Determination of the absolute configuration of optically active compounds by means of X-rays. Nature (London), 168, 271–272.Google Scholar
Blake, C. C. F., Johnson, L. N., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R. (1967). Crystallographic studies of the activity of hen egg-white lysozyme. Proc. R. Soc. London Ser. B, 167, 378–388.Google Scholar
Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R. (1965). Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution. Nature (London), 206, 757–761.Google Scholar
Blake, C. C. F., Mair, G. A., North, A. C. T., Phillips, D. C. & Sarma, V. R. (1967). On the conformation of the hen egg-white lysozyme molecule. Proc. R. Soc. London. Ser. B, 167, 365–377.Google Scholar
Bloomer, A. C., Champness, J. N., Bricogne, G., Staden, R. & Klug, A. (1978). Protein disk of tobacco mosaic virus at 2.8 Å resolution showing the interactions within and between subunits. Nature (London), 276, 362–368.Google Scholar
Blow, D. M. & Crick, F. H. C. (1959). The treatment of errors in the isomorphous replacement method. Acta Cryst. 12, 794–802.Google Scholar
Blow, D. M. & Rossmann, M. G. (1961). The single isomorphous replacement method. Acta Cryst. 14, 1195–1202.Google Scholar
Bluhm, M. M., Bodo, G., Dintzis, H. M. & Kendrew, J. C. (1958). The crystal structure of myoglobin. IV. A Fourier projection of sperm-whale myoglobin by the method of isomorphous replacement. Proc. R. Soc. London Ser. A, 246, 369–389.Google Scholar
Bodo, G., Dintzis, H. M., Kendrew, J. C. & Wyckoff, H. W. (1959). The crystal structure of myoglobin. V. A low-resolution three-dimensional Fourier synthesis of sperm-whale myoglobin crystals. Proc. R. Soc. London Ser. A, 253, 70–102.Google Scholar
Boyes-Watson, J., Davidson, E. & Perutz, M. F. (1947). An X-ray study of horse methaemoglobin. I. Proc. R. Soc. London Ser. A, 191, 83–132.Google Scholar
Bragg, L. & Perutz, M. F. (1952). The structure of haemoglobin. Proc. R. Soc. London Ser. A, 213, 425–435.Google Scholar
Bragg, W. H. (1915). X-rays and crystal structure. Philos. Trans. R. Soc. London Ser. A, 215, 253–274.Google Scholar
Bragg, W. H. & Bragg, W. L. (1913). The reflection of X-rays in crystals. Proc. R. Soc. London Ser. A, 88, 428–438.Google Scholar
Bragg, W. L. (1913). The structure of some crystals as indicated by their diffraction of X-rays. Proc. R. Soc. London Ser. A, 89, 248–277.Google Scholar
Bragg, W. L. (1929a). The determination of parameters in crystal structures by means of Fourier series. Proc. R. Soc. London Ser. A, 123, 537–559.Google Scholar
Bragg, W. L. (1929b). An optical method of representing the results of X-ray analysis. Z. Kristallogr. 70, 475–492.Google Scholar
Bragg, W. L. (1958). The determination of the coordinates of heavy atoms in protein crystals. Acta Cryst. 11, 70–75.Google Scholar
Bricogne, G. (1976). Methods and programs for direct-space exploitation of geometric redundancies. Acta Cryst. A32, 832–847.Google Scholar
Buehner, M., Ford, G. C., Moras, D., Olsen, K. W. & Rossmann, M. G. (1974). Structure determination of crystalline lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. Mol. Biol. 82, 563–585.Google Scholar
Chothia, C. (1973). Conformation of twisted β-pleated sheets in proteins. J. Mol. Biol. 75, 295–302.Google Scholar
Cochran, W., Crick, F. H. C. & Vand, V. (1952). The structure of synthetic polypeptides. I. The transform of atoms on a helix. Acta Cryst. 5, 581–586.Google Scholar
Crowfoot, D. (1948). X-ray crystallographic studies of compounds of biochemical interest. Annu. Rev. Biochem. 17, 115–146.Google Scholar
Crowfoot, D., Bunn, C. W., Rogers-Low, B. W. & Turner-Jones, A. (1949). The X-ray crystallographic investigation of the structure of penicillin. In The chemistry of penicillin, edited by H. T. Clarke, J. R. Johnson & R. Robinson, pp. 310–367. Princeton University Press.Google Scholar
Crowther, R. A. (1969). The use of non-crystallographic symmetry for phase determination. Acta Cryst. B25, 2571–2580.Google Scholar
Crowther, R. A. (1972). The fast rotation function. In The molecular replacement method, edited by M. G. Rossmann, pp. 173–178. New York: Gordon & Breach.Google Scholar
Cullis, A. F., Muirhead, H., Perutz, M. F., Rossmann, M. G. & North, A. C. T. (1962). The structure of haemoglobin. IX. A three-dimensional Fourier synthesis at 5.5 Å resolution: description of the structure. Proc. R. Soc. London Ser. A, 265, 161–187.Google Scholar
Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1985). Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature (London), 318, 618–624.Google Scholar
Dickerson, R. E., Kendrew, J. C. & Strandberg, B. E. (1961). The crystal structure of myoglobin: phase determination to a resolution of 2 Å by the method of isomorphous replacement. Acta Cryst. 14, 1188–1195.Google Scholar
Dickerson, R. E., Takano, T., Eisenberg, D., Kallai, O. B., Samson, L., Cooper, A. & Margoliash, E. (1971). Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 Å resolution. J. Biol. Chem. 246, 1511–1535.Google Scholar
Dodson, E., Harding, M. M., Hodgkin, D. C. & Rossmann, M. G. (1966). The crystal structure of insulin. III. Evidence for a 2-fold axis in rhombohedral zinc insulin. J. Mol. Biol. 16, 227–241.Google Scholar
Drenth, J., Hol, W. G. J., Jansonius, J. N. & Koekoek, R. (1972). A comparison of the three-dimensional structures of subtilisin BPN′ and subtilisin Novo. Cold Spring Harbor Symp. Quant. Biol. 36, 107–116.Google Scholar
Drenth, J., Jansonius, J. N., Koekoek, R., Swen, H. M. & Wolthers, B. G. (1968). Structure of papain. Nature (London), 218, 929–932.Google Scholar
Green, D. W., Ingram, V. M. & Perutz, M. F. (1954). The structure of haemoglobin. IV. Sign determination by the isomorphous replacement method. Proc. R. Soc. London Ser. A, 225, 287–307.Google Scholar
Hahn, Th. (2005). Editor. International tables for crystallography, Vol. A. Space-group symmetry. Heidelberg: Springer.Google Scholar
Harker, D. (1956). The determination of the phases of the structure factors of non-centrosymmetric crystals by the method of double isomorphous replacement. Acta Cryst. 9, 1–9.Google Scholar
Harker, D. & Kasper, J. S. (1947). Phases of Fourier coefficients directly from crystal diffraction data. J. Chem. Phys. 15, 882–884.Google Scholar
Harrison, S. C., Olson, A. J., Schutt, C. E., Winkler, F. K. & Bricogne, G. (1978). Tomato bushy stunt virus at 2.9 Å resolution. Nature (London), 276, 368–373.Google Scholar
Hendrickson, W. A. (1991). Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science, 254, 51–58.Google Scholar
Hendrickson, W. A. & Teeter, M. M. (1981). Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature (London), 290, 107–113.Google Scholar
Henry, N. F. M. & Lonsdale, K. (1952). Editors. International tables for X-ray crystallography, Vol. I. Symmetry groups. Birmingham: Kynoch Press.Google Scholar
Hermann, C. (1935). Editor. Internationale Tabellen zur Bestimmung von Kristallstrukturen, 1. Band. Gruppentheoretische Tafeln. Berlin: Begrüder Borntraeger.Google Scholar
Hilton, H. (1903). Mathematical crystallography and the theory of groups of movements. Oxford: Clarendon Press.Google Scholar
Hodgkin, D. C., Kamper, J., Lindsey, J., MacKay, M., Pickworth, J., Robertson, J. H., Shoemaker, C. B., White, J. G., Prosen, R. J. & Trueblood, K. N. (1957). The structure of vitamin B₁₂. I. An outline of the crystallographic investigation of vitamin B₁₂. Proc. R. Soc. London Ser. A, 242, 228–263.Google Scholar
Holm, L. & Sander, C. (1997). New structure – novel fold? Structure, 5, 165–171.Google Scholar
Holmes, K. C., Stubbs, G. J., Mandelkow, E. & Gallwitz, U. (1975). Structure of tobacco mosaic virus at 6.7 Å resolution. Nature (London), 254, 192–196.Google Scholar
Hooke, R. (1665). Micrographia, p. 85. London: Royal Society.Google Scholar
Huygens, C. (1690). Traité de la lumière. Leiden. (English translation by S. P. Thompson, 1912. London: Macmillan and Co.)Google Scholar
Jones, T. A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Cryst. 11, 268–272.Google Scholar
Judson, H. F. (1979). The eighth day of creation. New York: Simon & Schuster.Google Scholar
Kartha, G., Bello, J. & Harker, D. (1967). Tertiary structure of ribonuclease. Nature (London), 213, 862–865.Google Scholar
Kendrew, J. C., Bodo, G., Dintzis, H. M., Parrish, R. G., Wyckoff, H. & Phillips, D. C. (1958). A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature (London), 181, 662–666.Google Scholar
Kendrew, J. C., Dickerson, R. E., Strandberg, B. E., Hart, R. G., Davies, D. R., Phillips, D. C. & Shore, V. C. (1960). Structure of myoglobin. A three-dimensional Fourier synthesis at 2 Å resolution. Nature (London), 185, 422–427.Google Scholar
Kim, S. H., Quigley, G. J., Suddath, F. L., McPherson, A., Sneden, D., Kim, J. J., Weinzierl, J. & Rich, A. (1973). Three-dimensional structure of yeast phenylalanine transfer RNA: folding of the polynucleotide chain. Science, 179, 285–288.Google Scholar
Kraut, J., Robertus, J. D., Birktoft, J. J., Alden, R. A., Wilcox, P. E. & Powers, J. C. (1972). The aromatic substrate binding site in subtilisin BPN′ and its resemblance to chymotrypsin. Cold Spring Harbor Symp. Quant. Biol. 36, 117–123.Google Scholar
Linderström-Lang, K. U. & Schellman, J. A. (1959). Protein structure and enzyme activity. In The enzymes, edited by P. D. Boyer, Vol. 1, 2nd ed., pp. 443–510. New York: Academic Press.Google Scholar
Lipson, H. & Cochran, W. (1953). The determination of crystal structures, pp. 325–326. London: G. Bell and Sons Ltd.Google Scholar
Lonsdale, K. (1928). The structure of the benzene ring. Nature (London), 122, 810.Google Scholar
Lonsdale, K. (1936). Structure factor tables. London: Bell.Google Scholar
McLachlan, D. Jr & Champaygne, E. F. (1946). A machine for the application of sand in making Fourier projections of crystal structures. J. Appl. Phys. 17, 1006–1014.Google Scholar
Main, P. & Rossmann, M. G. (1966). Relationships among structure factors due to identical molecules in different crystallographic environments. Acta Cryst. 21, 67–72.Google Scholar
Matthews, B. W. (1966). The determination of the position of anomalously scattering heavy atom groups in protein crystals. Acta Cryst. 20, 230–239.Google Scholar
Matthews, B. W., Sigler, P. B., Henderson, R. & Blow, D. M. (1967). Three-dimensional structure of tosyl-α-chymotrypsin. Nature (London), 214, 652–656.Google Scholar
Murzin, A. G., Brenner, S. E., Hubbard, T. & Chothia, C. (1995). SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536–540.Google Scholar
North, A. C. T. (1965). The combination of isomorphous replacement and anomalous scattering data in phase determination of non-centrosymmetric reflexions. Acta Cryst. 18, 212–216.Google Scholar
Olby, R. (1974). The path to the double helix. Seattle: University of Washington Press.Google Scholar
Patterson, A. L. (1934). A Fourier series method for the determination of the components of interatomic distances in crystals. Phys. Rev. 46, 372–376.Google Scholar
Patterson, A. L. (1935). A direct method for the determination of the components of interatomic distances in crystals. Z. Kristallogr. 90, 517–542.Google Scholar
Pauling, L. & Corey, R. B. (1951). Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets. Proc. Natl Acad. Sci. USA, 37, 729–740.Google Scholar
Pauling, L., Corey, R. B. & Branson, H. R. (1951). The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl Acad. Sci. USA, 37, 205–211.Google Scholar
Pepinsky, R. (1947). An electronic computer for X-ray crystal structure analysis. J. Appl. Phys. 18, 601–604.Google Scholar
Perutz, M. F. (1946). Trans. Faraday Soc. 42B, 187.Google Scholar
Perutz, M. F. (1949). An X-ray study of horse methaemoglobin. II. Proc. R. Soc. London Ser. A, 195, 474–499.Google Scholar
Perutz, M. F. (1951a). New X-ray evidence on the configuration of polypeptide chains. Nature (London), 167, 1053–1054.Google Scholar
Perutz, M. F. (1951b). The 1.5-A. reflextion from proteins and polypeptides. Nature (London), 168, 653–654.Google Scholar
Perutz, M. F. (1954). The structure of haemoglobin. III. Direct determination of the molecular transform. Proc. R. Soc. London Ser. A, 225, 264–286.Google Scholar
Perutz, M. F. (1956). Isomorphous replacement and phase determination in non-centrosymmetric space groups. Acta Cryst. 9, 867–873.Google Scholar
Perutz, M. F. (1962). Proteins and nucleic acids. Structure and function. Amsterdam: Elsevier Publishing Co.Google Scholar
Perutz, M. F. (1997). Keilin and the molteno. In Selected topics in the history of biochemistry: personal reflections, V, edited by G. Semenza & R. Jaenicke, pp. 57–67. Amsterdam: Elsevier.Google Scholar
Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775–791.Google Scholar
Ramachandran, G. N. & Sasisekharan, V. (1968). Conformation of polypeptides and proteins. Adv. Protein Chem. 23, 283–438.Google Scholar
Reeke, G. N., Hartsuck, J. A., Ludwig, M. L., Quiocho, F. A., Steitz, T. A. & Lipscomb, W. N. (1967). The structure of carboxypeptidase A, VI. Some results at 2.0-Å resolution, and the complex with glycyl-tyrosine at 2.8-Å resolution. Proc. Natl Acad. Sci. USA, 58, 2220–2226.Google Scholar
Richards, F. M. (1968). The matching of physical models to three-dimensional electron-density maps: a simple optical device. J. Mol. Biol. 37, 225–230.Google Scholar
Richardson, J. S. (1977). β-Sheet topology and the relatedness of proteins. Nature (London), 268, 495–500.Google Scholar
Robertson, J. M. (1935). An X-ray study of the structure of phthalocyanines. Part I. The metal-free, nickel, copper, and platinum compounds. J. Chem. Soc. pp. 615–621.Google Scholar
Robertson, J. M. (1936). Numerical and mechanical methods in double Fourier synthesis. Philos. Mag. 21, 176–187.Google Scholar
Robertus, J. D., Ladner, J. E., Finch, J. T., Rhodes, D., Brown, R. S., Clark, B. F. C. & Klug, A. (1974). Structure of yeast phenylalanine tRNA at 3 Å resolution. Nature (London), 250, 546–551.Google Scholar
Rossmann, M. G. (1960). The accurate determination of the position and shape of heavy-atom replacement groups in proteins. Acta Cryst. 13, 221–226.Google Scholar
Rossmann, M. G. (1961). The position of anomalous scatterers in protein crystals. Acta Cryst. 14, 383–388.Google Scholar
Rossmann, M. G. (1972). Editor. The molecular replacement method. New York: Gordon & Breach.Google Scholar
Rossmann, M. G., Arnold, E., Erickson, J. W., Frankenberger, E. A., Griffith, J. P., Hecht, H. J., Johnson, J. E., Kamer, G., Luo, M., Mosser, A. G., Rueckert, R. R., Sherry, B. & Vriend, G. (1985). Structure of a human common cold virus and functional relationship to other picornaviruses. Nature (London), 317, 145–153.Google Scholar
Rossmann, M. G. & Blow, D. M. (1962). The detection of sub-units within the crystallographic asymmetric unit. Acta Cryst. 15, 24–31.Google Scholar
Rossmann, M. G. & Blow, D. M. (1963). Determination of phases by the conditions of non-crystallographic symmetry. Acta Cryst. 16, 39–45.Google Scholar
Rossmann, M. G., Moras, D. & Olsen, K. W. (1974). Chemical and biological evolution of a nucleotide-binding protein. Nature (London), 250, 194–199.Google Scholar
Sanger, F. & Thompson, E. O. P. (1953a). The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysates. Biochem. J. 53, 353–366.Google Scholar
Sanger, F. & Thompson, E. O. P. (1953b). The amino-acid sequence in the glycyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 53, 366–374.Google Scholar
Sanger, F. & Tuppy, H. (1951). The amino-acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochem. J. 49, 481–490.Google Scholar
Schoenflies, A. M. (1891). Krystallsysteme und Krystallstruktur. Leipzig: Druck und Verlag von B. G. Teubner.Google Scholar
Snow, C. P. (1934). The search. Indianapolis and New York: Bobbs-Merrill Co.Google Scholar
Watson, J. D. (1954). The structure of tobacco mosaic virus. I. X-ray evidence of a helical arrangement of sub-units around the longitudinal axis. Biochim. Biophys. Acta, 13, 10–19.Google Scholar
Watson, J. D. (1968). The double helix. New York: Atheneum.Google Scholar
Wyckoff, H. W., Hardman, K. D., Allewell, N. M., Inagami, T., Johnson, L. N. & Richards, F. M. (1967). The structure of ribonuclease-S at 3.5 Å resolution. J. Biol. Chem. 242, 3984–3988.Google Scholar