About the Author - Peter Nollert

Peter Nollert

I'm Peter Nollert and I write this blog to point researchers to topics that are relevant to protein crystallization. My mission is to help spread knowledge that is 'out there on the web' and help you succeed with your protein structure research.  I oversee the membrane protein research and technology development activities at Emerald BioStructures. Check out The GPCR blog, or my publications

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Protein Crystallization Hits

Best of 25 hottest articles from STRUCTURE

by Peter Nollert
April 14, 2010 03:45

Structure, the magazine, sent me an email the other day with "the most requested full text articles your colleagues and competitors are currently downloading from Structure.". OK - let's see what's there for us protein crystallizers:

  1. Conformation Dependence of Backbone Geometry in Proteins
  2. Structure of the Human Dicer-TRBP Complex by Electron Microscopy
  3. The Nuclear Pore Complex Has Entered the Atomic Age • Review article
  4. Discovery Through the Computational Microscope • Review article
  5. Structure of PAS-Linked Histidine Kinase and the Response Regulator Complex
  6. Structure of IL-33 and Its Interaction with the ST2 and IL-1RAcP Receptors-Insight into Heterotrimeric IL-1 Signaling Complexes
  7. Insights into How Nucleotide-Binding Domains Power ABC Transport
  8. Structural Insights on the Mycobacterium tuberculosis Proteasomal ATPase Mpa
  9. Fluorescence-Detection Size-Exclusion Chromatography for Precrystallization Screening of Integral Membrane Proteins
  10. Secondary Structure of Huntingtin Amino-Terminal Region
  11. Structure and Signaling Mechanism of Per-ARNT-Sim Domains • Review article
  12. Intrinsic Domain and Loop Dynamics Commensurate with Catalytic Turnover in an Induced-Fit Enzyme
  13. Quantitative Determination of the Conformational Properties of Partially Folded and Intrinsically Disordered Proteins Using NMR Dipolar Couplings • Review article
  14. Structural Plasticity of Eph Receptor A4 Facilitates Cross-Class Ephrin Signaling
  15. Structural Dynamics of Light-Driven Proton Pumps
  16. Subunit Architecture of Multiprotein Assemblies Determined Using Restraints from Gas-Phase Measurements
  17. Toward Structural Elucidation of the @c-Secretase Complex • Review article
  18. Structural Basis for DNase Activity of a Conserved Protein Implicated in CRISPR-Mediated Genome Defense
  19. Structural Basis of Novel Interactions Between the Small-GTPase and GDI-like Domains in Prokaryotic FeoB Iron Transporter
  20. Structures and mechanisms of glycosyl hydrolases
  21. Binding of Small-Molecule Ligands to Proteins:''What You See''Is Not Always''What You Get'' • Review article
  22. Structural Basis for Calcium Sensing by GCaMP2
  23. Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases
  24. The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways • Review article
  25. A Specific Cholesterol Binding Site Is Established by the 2.8 A Structure of the Human @b"2-Adrenergic Receptor

I am rather surprised by the high number of membrane protein-related papers. Out of these 25 hottest STRUCTURE articles I'd say that #9 looks like the most interesting one:

T. Kawate & E. Gouaux (2006)
Fluorescence-Detection Size-Exclusion Chromatography for Precrystallization Screening of Integral Membrane Proteins
Volume 14 (4), 673-681

And this is of course Eric Gouaux & Toshimitsu Kawate's clever paper on analyzing the monodispersity and stability of protein-detergent complexes: 

Schematic pre-crystalline screening for membrane protein crystallization.

Described is a "rapid and efficient precrystallization screening strategy in which the target protein is covalently fused to green fluorescent protein (GFP) and the resulting unpurified protein is analyzed by fluorescence-detection size-exclusion chromatography (FSEC). This strategy requires only nanogram quantities of unpurified protein and allows one to evaluate localization and expression level, the degree of monodispersity, and the approximate molecular mass." This helps leapfrogging the otherwise tedious step purification optimization. And it helps to reduce "...unproductive large-scale protein expression and purification..." efforts.

Well done!

Peter

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