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Crystallization and preliminary crystallographic studies of the precursor and mature forms of a neutral lipase from the fungus Rhizopus delemar
Author(s) -
Swenson Lora,
Green Ruth,
Joerger Rolf,
Haas Michael,
Scott Karen,
Wei Yunyi,
Derewenda Urszula,
Lawson David M.,
Derewenda Zygmunt S.
Publication year - 1994
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.340180311
Subject(s) - lipase , orthorhombic crystal system , monoclinic crystal system , crystallization , molecule , crystallography , chemistry , crystal (programming language) , diad , stereochemistry , crystal structure , enzyme , polymer , organic chemistry , computer science , programming language , copolymer
A neutral lipase from the filamentous fungus Rhizopus delemar has been crystallized in both its proenzyme and mature forms. Although the latter crystallizes readily and produces a variety of crystal forms, only one was found to be suitable for X‐ray studies. It is monoclinic ( C 2, a = 92.8 Å, b = 128.9 Å, c = 78.3 Å, β = 135.8) with two molecules in the asymmetric unit related by a noncrystallographic diad. The prolipase crystals are orthorhombic ( P 2 1 2 1 2 1 , with a = 79.8 Å, b = 115.2 Å, c = 73.0 Å) and also contain a pair of molecules in the asymmetric unit. Initial results of molecular replacement calculations using the refined coordinates of the related lipase from Rhizomucor miehei identified the correct orientations and positions of the protein molecules in the unit cells of crystals of both proenzyme and the mature form. © 1994 John Wiley & Sons, Inc.