Structural Biochemistry A


This curricular unit will provide the students with theoretical and practical skills to:

  • plan, execute and analyze protein crystallization assays;
  • carry out a crystallographic characterization of the crystals obtained;
  • collect and process diffraction data from a protein crystal;
  • plan and execute the 3D structure determination of a protein;
  • build, refine and critically analyze the 3D structural model of a protein;
  • perform the structural analysis of the model obtained, compare it with models obtained by other methods and find similar structures in databases;
  • carry out a basic interpretation of 1D and 2D NMR spectra of proteins;
  • collect and process 1D and 2D NMR spectra of proteins;
  • determine by NMR the structure of a protein with MW < 15 kDa

General characterization





Responsible teacher

Pedro Manuel Henriques Marques Matias, Ricardo Saraiva Loureiro Oliveira Louro


Weekly - 4

Total - Available soon

Teaching language



Available soon


“Crystallography made Crystal Clear - A Guide for users of Macromolecular Models” G. Rhodes, 2nd Ed., Academic Press: San Diego, London (2000)

“Introduction to Protein Structure”  Branden, C.-I. & Tooze, J. Garland Pub. (1999)

“Structural Biology; Practical NMR applications” Q. Teng, Springer Science +Business Media, Inc, NY (2005)

Wlodawer, A., Minor, W., Dauter, Z., and Jaskolski, M. (2008) "Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures", FEBS J 275, 1-21. doi:10.1111/j.1742-4658.2007.06178.x

Teaching method

Available soon

Evaluation method

Available soon

Subject matter

  • Crystal symmetry; crystallization methods; characterization of crystals;
  • sources of X-rays, diffraction by single crystals, instruments and methods for diffraction data collection;
  • The structure factor, electron density maps, the "phase problem" and methods for its solution;
  • Methods for building and refining a crystallographic structural model; convergence criteria;
  • Electron Crystallography and Electron Microscopy for 3D structure analysis;
  • Validation methods for crystallographic protein 3D structures; structural comparison; crystallographic databases. Comparison with other methods of 3D structural analysis. On-line computational tools;
  • Basic theory of 1D and 2D NMR. Structural information: angles, distances, chemical environment.
  • Pulse sequences for data acquisition and spectral assignment. 2D and 3D methods.
  • Protein structure determination methods by NMR: Proteins with MW15kDa.


Programs where the course is taught: