DNA-binding domain of myelin-gene regulatory factor: purification, crystallization and X-ray analysis

In this study, the MRF DBD was cloned, purified and crystallized in order to understand the molecular mechanism that regulates the transcription of myelin genes. Selenomethionine was subsequently introduced into the crystals to obtain the phases for the MRF DBD structure. The native and selenomethionine-labelled crystals exhibited diffraction to 2.50 and 2.51   Å resolution, respectively. The crystals belonged to space group P321 and the selenomethionine-labelled crystals had unit-cell parameters a = 104.0, b = 104.0, c = 46.7   Å , α = 90, β = 90, γ = 120 ° . The calculated Matthews coefficient was 3.04   Å 3 Da − 1 and the solvent content was 59.5%, indicating the presence of one MRF DBD molecule in the asymmetric unit.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: myelin-gene regulation MRF DNA-binding domain trimeric transcription factor X-ray crystallography research communications Source Type: research