 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](nq5002fig1mag.jpg)
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Figure 1
Purification of a protein fraction from L. muta venom. (a) Ion-exchange chromatography (IEX) profile on a CM Sephadex C-50 column. Several protein peaks were eluted both prior to and during the NaCl gradient (0–1 M), expressed in column volumes (CV) and indicated by the blue line. Peak 3 (81–101 ml) was selected for further purification as part of a broader fractionation aimed at isolating pure components for crystallization trials. (b) Size-exclusion chromatography (SEC) profile of peak 3 on a Superdex 200 16/60 column. The elution profile displays three peaks, with the most intense peak (highlighted as a shaded region and indicated by the arrow) containing a protein of approximately 13 kDa, as confirmed by 15% SDS–PAGE (lane M, molecular-weight marker, inset). The molecular-weight marker and the protein band correspond to different lanes from the same SDS–PAGE gel; the image was cropped and rearranged for clarity. This fraction was subsequently used for structural studies and for PLA2 activity measurements. |
![[Figure 1]](nq5002fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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