 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](bw5087fig1mag.jpg)
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Figure 1
Purification of the refolded complex of Mamu-A*01 heavy chain with human β2m and SIV Gag_CM9 peptide by FPLC Superdex G75 gel-filtration and Resouce-Q anion-exchange chromatography (Amersham). (a) Gel-filtration profile of the refolded products. Peak 1 represents aggregated heavy chain, peak 2 represents the correctly refolded complex (45 kDa) and peak 3 represents the abundant β2m. (b) Reduced SDS–PAGE gel (15%) of the purified proteins. The left column corresponds to molecular-weight markers. The line labelled 1 represents the peak 1, line 2 represents the peak 2 and line 3 represents the peak 3 fractions. (c) Results of further purification of the refolded complex (peak 2) by anion exchange. Peak 4 represents the Mamu-A*01 complex, which was eluted at an NaCl concentration of 14–25 mM. Peak 5 represents the different charged complex eluted using a higher concentration of salt. Inset: reduced SDS–PAGE gel (15%) for peak 4. |
![[Figure 1]](bw5087fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
