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Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L.

ABSTRACT: Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase Hrd1, plays an important role in selecting and transporting ERAD substrates for degradation in the endoplasmic reticulum. In this study, the purification, crystallization and preliminary X-ray diffraction analysis of recombinant mouse SEL1L (residues 348-533) are reported. The crystals were obtained by the hanging-drop vapour-diffusion method at pH 8.5 and 277 K using 30% 2-propanol as a precipitant. Optimized crystals diffracted to 3.3 Å resolution at a synchrotron-radiation source. Preliminary X-ray diffraction analysis revealed that the crystals belonged to space group P21 and contained four molecules per asymmetric unit, with a solvent content of 44%.

SUBMITTER: Jeong H

PROVIDER: S-EPMC4259226 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L.

Jeong Hanbin H Lee Hakbong H Lee Changwook C

Acta crystallographica. Section F, Structural biology communications 20141114 Pt 12

Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase Hrd1, plays an important role in selecting and transporting ERAD substrates for degradation in the endoplasmic reticulum. In this study, the purification, crystallization and preliminary X-ray diffraction analysis of recombinant mouse SEL1L (resid ...[more]

PMID: 25484212

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