Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics.
Cost and time reduction are two of the driving forces in the development of new strategies for protein crystallization and subsequent structure determination. Here, we report the analysis of the Thermotoga maritima proteome, in which we compare the proteins that were successfully expressed, purified and crystallized versus the rest of the proteome. This set of almost 500 proteins represents one of the largest, internally consistent, protein expression and crystallization datasets available. The analysis shows that individual parameters, such as isoelectric point, sequence length, average hydropathy, low complexity regions (SEG), and combinations of these biophysical properties for crystallized proteins define a distinct subset of the T. maritima proteome. The distribution profiles of the various biophysical properties in the expression/crystallization set are then used to extract rules to improve target selection and improve the efficiency and output of structural genomics, as well as general structural biology efforts.
Canaves
Jaume M
JM
The Joint Center for Structural Genomics, USA.
Page
Rebecca
R
Wilson
Ian A
IA
Stevens
Raymond C
RC
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D007526:Isoelectric Point; D016366:Open Reading Frames; D011487:Protein Conformation; D021382:Protein Sorting Signals; D020543:Proteome / Q000032:analysis*; D020124:Thermotoga maritima / Q000737:chemistry* / Q000235:genetics
D000596:Amino Acids; D001426:Bacterial Proteins; D021382:Protein Sorting Signals; D020543:Proteome