Premium
Crystallization and preliminary X‐ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major
Author(s) -
Schlagenhauf Edith,
Etges Robert,
Metcalf Peter
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220109
Subject(s) - monoclinic crystal system , crystallography , crystallization , molecular replacement , tetragonal crystal system , x ray crystallography , crystal (programming language) , molecule , crystal structure , chemistry , diffraction , resolution (logic) , single crystal , materials science , physics , optics , organic chemistry , programming language , artificial intelligence , computer science
The membrane‐bound GPI‐anchored zinc metalloproteinase leishmanolysin purified from Leishmania major promastigotes has been crystallized in its mature form. Two crystal forms of leishmanolysin have been grown by the vapor diffusion method using 2‐methyl‐2,4‐pentanediol as the precipitant. Macroseeding techniques were employed to produce large single crystals. Protein microhet‐erogeneity in molecular size and charge was incorporated into both crystal forms. The tetragonal crystal form belongs to the space group P 4 1 2 1 2 or the enantiomorph P 4 3 2 1 2, has unit cell parameters of a = b = 63.6 Å, c = 251.4 Å, and contains one molecule per asymmetric unit. The second crystal form is monoclinic, space group C 2, with unit cell dimensions a = 107.2 Å, b = 90.6 Å, c = 70.6 Å, β = 110.6°, and also contains one molecule per asymmetric unit. Both crystal forms diffract X‐rays beyond 2.6 Å resolution and are suitable for X‐ray analysis. Native diffraction data sets have been collected and the structure determination of leishmanolysin using a combination of the isomorphous replacement and the molecular replacement methods is in progress. © 1995 Wiley‐Liss, Inc.