The total synthesis of proteins as enzymes was one of the 'Grand Challenges' of 20th century chemistry. Despite decades of development by skilled organic chemists throughout the world, conventional synthetic methods were able to make only the smallest proteins. The field of synthetic protein chemistry was stuck and a radical change was needed to unstick it. In 1992 we introduced the 'chemical ligation’ concept: chemoselective reaction forming an analogue structure linking two unprotected synthetic peptide segments.[1] Then, in 1994 we introduced native chemical ligation: thioester-mediated chemoselective condensation of unprotected peptides to give a native peptide bond linking two peptide segments.[2] The chemical ligation concept as realized in native chemical ligation forms the basis of modern  methods that enable the practical total chemical synthesis of proteins, including enzymes.[3] Synthetic products are characterized at high resolution by LCMS  for purity and covalent structure, by multidimensional NMR for unique fold, and by X-ray crystallography to reveal the tertiary structure of the synthetic protein molecule. Chemical protein synthesis gives precise, atom-by-atom control over the covalent structure of a protein molecule and enables the incorporation of a wide range of non-coded building blocks and the introduction of isotope labels with single atom precision. I will present case studies to illustrate the utility of chemical protein synthesis applied to targets including the HIV-1 protease,[4] EPO,[5]  a D-protein antagonist of VEGF-A,[6] ester insulin,[7] and to the design, synthesis and structure elucidation of a protein molecule of unprecedented covalent topology.[8] Novel features of these examples include the preparation of D-protein molecules and the use of racemic crystallography for protein structure determination.[9] Current and future applications of chemical synthesis to quasi-racemic crystallography of (neo)glycoproteins will be discussed.