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The high-throughput protein-to-structure pipeline at SECSG.

Publication ,  Journal Article
Liu, Z-J; Tempel, W; Ng, JD; Lin, D; Shah, AK; Chen, L; Horanyi, PS; Habel, JE; Kataeva, IA; Xu, H; Yang, H; Chang, JC; Huang, L; Chang, S-H ...
Published in: Acta Crystallogr D Biol Crystallogr
June 2005

Using a high degree of automation, the crystallography core at the Southeast Collaboratory for Structural Genomics (SECSG) has developed a high-throughput protein-to-structure pipeline. Various robots and automation procedures have been adopted and integrated into a pipeline that is capable of screening 40 proteins for crystallization and solving four protein structures per week. This pipeline is composed of three major units: crystallization, structure determination/validation and crystallomics. Coupled with the protein-production cores at SECSG, the protein-to-structure pipeline provides a two-tiered approach for protein production at SECSG. In tier 1, all protein samples supplied by the protein-production cores pass through the pipeline using standard crystallization screening and optimization procedures. The protein targets that failed to yield diffraction-quality crystals (resolution better than 3.0 A) become tier 2 or salvaging targets. The goal of tier 2 target salvaging, carried out by the crystallomics core, is to produce the target proteins with increased purity and homogeneity, which would render them more likely to yield well diffracting crystals. This is performed by alternative purification procedures and/or the introduction of chemical modifications to the proteins (such as tag removal, methylation, surface mutagenesis, selenomethionine labelling etc.). Details of the various procedures in the pipeline for protein crystallization, target salvaging, data collection/processing and high-throughput structure determination/validation, as well as some examples, are described.

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Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

June 2005

Volume

61

Issue

Pt 6

Start / End Page

679 / 684

Location

United States

Related Subject Headings

  • Proteins
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences
  • 03 Chemical Sciences
  • 02 Physical Sciences
 

Citation

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Liu, Z.-J., Tempel, W., Ng, J. D., Lin, D., Shah, A. K., Chen, L., … Wang, B.-C. (2005). The high-throughput protein-to-structure pipeline at SECSG. Acta Crystallogr D Biol Crystallogr, 61(Pt 6), 679–684. https://doi.org/10.1107/S0907444905013132
Liu, Zhi-Jie, Wolfram Tempel, Joseph D. Ng, Dawei Lin, Ashit K. Shah, Lirong Chen, Peter S. Horanyi, et al. “The high-throughput protein-to-structure pipeline at SECSG.Acta Crystallogr D Biol Crystallogr 61, no. Pt 6 (June 2005): 679–84. https://doi.org/10.1107/S0907444905013132.
Liu Z-J, Tempel W, Ng JD, Lin D, Shah AK, Chen L, et al. The high-throughput protein-to-structure pipeline at SECSG. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):679–84.
Liu, Zhi-Jie, et al. “The high-throughput protein-to-structure pipeline at SECSG.Acta Crystallogr D Biol Crystallogr, vol. 61, no. Pt 6, June 2005, pp. 679–84. Pubmed, doi:10.1107/S0907444905013132.
Liu Z-J, Tempel W, Ng JD, Lin D, Shah AK, Chen L, Horanyi PS, Habel JE, Kataeva IA, Xu H, Yang H, Chang JC, Huang L, Chang S-H, Zhou W, Lee D, Praissman JL, Zhang H, Newton MG, Rose JP, Richardson JS, Richardson DC, Wang B-C. The high-throughput protein-to-structure pipeline at SECSG. Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):679–684.
Journal cover image

Published In

Acta Crystallogr D Biol Crystallogr

DOI

ISSN

0907-4449

Publication Date

June 2005

Volume

61

Issue

Pt 6

Start / End Page

679 / 684

Location

United States

Related Subject Headings

  • Proteins
  • Crystallography, X-Ray
  • Crystallization
  • Biophysics
  • 51 Physical sciences
  • 34 Chemical sciences
  • 31 Biological sciences
  • 06 Biological Sciences
  • 03 Chemical Sciences
  • 02 Physical Sciences