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Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin‐related protein 3
Author(s) -
Son Ji Young,
Lee Jee Un,
Yoo KiYoung,
Shin Woori,
Im DongWon,
Kim Seung Jun,
Ryu Seong Eon,
Heo YongSeok
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14015714
Subject(s) - crystallization , crystallography , expression (computer science) , materials science , computational biology , chemistry , computer science , biology , programming language , organic chemistry
Myotubularin‐related proteins are a large family of phosphatases that have the catalytic activity of dephosphorylating the phospholipid molecules phosphatidylinositol 3‐phosphate and phosphatidylinositol 3,5‐bisphosphate. Each of the 14 family members contains a phosphatase catalytic domain, which is inactive in six family members owing to amino‐acid changes in a key motif for the activity. All of the members also bear PH‐GRAM domains, which have low homologies between them and have roles that are not yet clear. Here, the cloning, expression, purification and crystallization of human myotubularin‐related protein 3 encompassing the PH‐GRAM and the phosphatase catalytic domain are reported. Preliminary X‐ray crystallographic analysis shows that the crystals diffracted to 3.30 Å resolution at a synchrotron X‐ray source. The crystals belonged to space group C 2, with unit‐cell parameters a = 323.3, b = 263.3, c = 149.4 Å, β = 109.7°.