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Purification, crystallization and preliminary crystallographic analysis of the CBS domain protein MJ1004 from Methanocaldococcus jannaschii.Purification, crystallization and preliminary crystallographic analysis of the CBS domain protein MJ1004 from Methanocaldococcus jannaschii.Oyenarte I, Lucas M, Gomez-García I, Martínez-Cruz LA. Acta Crystallogr Sect F, 2011 Mar 1; 67(3):318-24. doi: 10.1107/S17443091100534792011-02-28T23:00:00Z<p style="text-align:justify;"><span class="ms-rteThemeForeColor-2-5 ms-rteThemeFontFace-1 ms-rteFontSize-2">​<span style="font-weight:bold;">Abstract</span></span></p><div style="color:#000000;font-family:arial, helvetica, clean, sans-serif;text-align:justify;"><p style="margin-bottom:0.5em;font-size:1.04em;"><span class="ms-rteThemeFontFace-1 ms-rteFontSize-2">The purification and preliminary crystallographic analysis of the archaeal CBS-domain protein MJ1004 from Methanocaldococcus jannaschii are described. The native protein was overexpressed, purified and crystallized in the monoclinic space group P2(1), with unit-cell parameters a=54.4, b=53.8, c=82.6 Å, β=106.1°. The crystals diffracted X-rays to 2.7 Å resolution using synchrotron radiation. Matthews-volume calculations suggested the presence of two molecules in the asymmetric unit that are likely to correspond to a dimeric species, which is also observed in solution.</span><br></p></div><p>​<a href="https://www.ncbi.nlm.nih.gov/pubmed/21393835">[PubMed]</a><br></p>146