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Incorporating high‐throughput proteomics experiments into structural biology pipelines: Identification of the low‐hanging fruits
Author(s) -
Pache Roland A.,
Aloy Patrick
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700966
Subject(s) - proteomics , computational biology , identification (biology) , throughput , structural biology , structural genomics , biology , nanotechnology , computer science , biochemical engineering , protein structure , biochemistry , engineering , materials science , gene , ecology , telecommunications , wireless
The last years have seen the emergence of many large‐scale proteomics initiatives that have identified thousands of new protein interactions and macromolecular assemblies. However, unfortunately, only a few among the discovered complexes meet the high‐quality standards required to be promptly used in structural studies. This has thus created an increasing gap between the number of known protein interactions and complexes and those for which a high‐resolution 3‐D structure is available. Here, we present and validate a computational strategy to distinguish those complexes found in high‐throughput affinity purification experiments that will stand the best chances to successfully express, purify and crystallize with little further intervention. Our method suggests that there are some 50 complexes recently discovered in yeast that could readily enter the structural biology pipelines.