Premium
Crystallisation and preliminary X‐ray analysis of the ‘common‐type’ acylphosphatase
Author(s) -
Thunnissen Marjolein M.G.M.,
Agango Elisha G.,
Taddei Niccolò,
Liguri Gianfranco,
Cecchi Cristina,
Pieri Alessandro,
Ramponi Giampietro,
Nordlund Pär
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00363-e
Subject(s) - crystallization , crystallography , monomer , resolution (logic) , chemistry , x ray , diffraction , x ray crystallography , type (biology) , physics , optics , biology , organic chemistry , polymer , computer science , ecology , artificial intelligence
Single crystals of a ‘common‐type’ acylphosphatase from bovine testis have been grown. Crystals belong to space group C2 and have cell dimensions , , and β = 104.8 and contain one monomer per asymmetric unit. The crystals diffract better than 2.0 Å resolution and are well suited for an X‐ray structure determination.