 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ow5028fig1mag.jpg)
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Figure 1
Purification and crystallization of the human TLDc domain. (a) Elution profile of the purified TLDc domain on a Superdex 75 10/300 GL Increase column. The elution volume of 13.4 ml attests to the presence of a monomer in solution. (b) Coomassie Blue-stained SDS polyacrylamide gel electrophoresis of TLDc performed after the last step of purification by size-exclusion chromatography (10 µg protein; right lane). The left lane contains molecular-mass markers (labelled in kDa). (c) Crystals of the TLDc domain obtained in a sitting drop using PEG 300 as a precipitant. Crystals reached their final size (about 100–200 µm) within two days. (d) Asymmetric unit composition. Six monomers are present in the asymmetric unit, forming two superposed stable trimers as predicted by the PISA server (https://www.ebi.ac.uk/pdbe/pisa/). Chains A, B and D and chains C, E and F form the two assemblies. |
![[Figure 1]](ow5028fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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