Structure of the 30s Ribosomal Subunit in Nature, Vol. 407, 21 September 2000, pp. 327-339 (Wimberly, Brodersen, Clemons, Morgan-Warren, Carter, Vonrhein, Hartxch, Ramakrishnan); WITH Structure of Functionally Activated Small Ribosomal Subunit at 3.3 A Resolution in Cell Vol. 102, September 1, 2000, pp. 615-623 (Schluenzen, Tocilj, Zarivach, Harms, Gluehmann, Janell, Bashan, Bartels, Agmon, Franceschi, Yonath); WITH The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 A Resolution in Science, Vol. 289, 11 August 2000, pp. 905-920 (Ban, Nissen, Hansen, Moore, Steitz); WITH The Structural Basis of Ribosome Activity in Peptide Bond Synthesis in Science, Vol. 289, 11 August 2000, pp. 920-930. 2000 (Nissen, Hansen, Ban, Moore, and Steitz). Venkatraman Ramakrishnan, Thomas A. Steitz, Ilana Agmon Ada E. Yonath. Brian T. Wimberly. Ditlev E. Brodersen. William M. Clemons. Robert J. Morgan-Warren. Adrew P. Carter. Clemens Vonrhein. Thomas Hatsch. Frank Schluenzen. Ante Tocilj. Raz Zarivach. Joerg Harms. Marco Gluehmann. Daniela Janell. Anat Bashan. Heike Bartels, Francois Franceschi. Nenad Ban. Poul Nissen. Jeffrey Hansen. Peter B. Moore.

Structure of the 30s Ribosomal Subunit in Nature, Vol. 407, 21 September 2000, pp. 327-339 (Wimberly, Brodersen, Clemons, Morgan-Warren, Carter, Vonrhein, Hartxch, Ramakrishnan); WITH Structure of Functionally Activated Small Ribosomal Subunit at 3.3 A Resolution in Cell Vol. 102, September 1, 2000, pp. 615-623 (Schluenzen, Tocilj, Zarivach, Harms, Gluehmann, Janell, Bashan, Bartels, Agmon, Franceschi, Yonath); WITH The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 A Resolution in Science, Vol. 289, 11 August 2000, pp. 905-920 (Ban, Nissen, Hansen, Moore, Steitz); WITH The Structural Basis of Ribosome Activity in Peptide Bond Synthesis in Science, Vol. 289, 11 August 2000, pp. 920-930. 2000 (Nissen, Hansen, Ban, Moore, and Steitz)

2000. 1st Edition. FIRST EDITIONS IN ORIGINAL WRAPS OF THE THREE NOBEL PRIZE WINNING PAPERS IN WHICH “PERHAPS THE MOST COMPLICATED WELL-DEFINED STRUCTURE IN OUR UNIVERSE” IS SOLVED, THE STRUCTURE OF THE RIBOSOME (Zou, Electron Crystallography, 18). “The 2009 Nobel Prize in Chemistry awards Venkatraman Ramakrishnan, Thomas A. Steitz and Ada E. Yonath for having showed what the ribosome looks like and how it functions at the atomic level. All three have used a method called X-ray crystallography to map the position for each and every one of the hundreds of thousands of atoms that make up the ribosome” (Nobel Prize Committee).

Present are the four papers in which three scientists, working independently, show how information encoded on strands of DNA is then translated in the thousands of proteins that make up all living matter. “This year's three Laureates have all generated 3D models that show how different antibiotics bind to the ribosome. These models are now used by scientists in order to develop new antibiotics, directly assisting the saving of lives and decreasing humanity's suffering” (Nobel Prize Committee).

Crystallography was revolutionized in early 1912 by the work of Max von Laue and his son Bragg who together proved that crystals could diffract X-rays. Throughout the 20th century, “hundreds of thousands of crystal structures were determined by crystallography, ranging from minerals and alloys over organic molecules to proteins and DNA” (Zou, Electron Crystallography, 18).

While we know that DNA molecules contain the blueprints for how human, plant, or bacterium looks and functions, the molecule itself remains passive; absent something else, life would not exist. “The blueprints become transformed into living matter through the work of ribosomes. Based upon the information in DNA, ribosomes make proteins: oxygen-transporting haemoglobin, antibodies of the immune system, hormones such as insulin, the collagen of the skin, or enzymes that break down sugar. There are tens of thousands of proteins in the body and they all have different forms and functions. They build and control life at the chemical level.

“An understanding of the ribosome's innermost workings is important for a scientific understanding of life. This knowledge can be put to a practical and immediate use; many of today's antibiotics cure various diseases by blocking the function of bacterial ribosomes. Without functional ribosomes, bacteria cannot survive. This is why ribosomes are such an important target for new antibiotics” (ibid). Item #760

CONDITION & DETAILS: 3 full issues in original wraps; one each of the journals Nature, Cell, and Science. 4to. Tear to rear of Nature issue archivally repaired, cover edge wear, minimal creases. No address labels. Each is tightly and solidly bound. Bright and clean inside and out. Near fine condition.

Price: $525.00