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Crystallization and preliminary X-ray analysis of carnein, a serine protease from Ipomoea carnea

By Ashok Kumar Patel, Niels van Oosterwijk, Vijay Kumar Singh, Henriëtte J. Rozeboom, Kor H. Kalk, Roland J. Siezen, Medicherla V. Jagannadham and Bauke W. Dijkstra

Abstract

Carnein is an 80 kDa subtilisin-like serine protease from the latex of the plant Ipomoea carnea which displays an exceptional resistance to chemical and thermal denaturation. In order to obtain the first crystal structure of a plant subtilisin and to gain insight into the structural determinants underlying its remarkable stability, carnein was isolated from I. carnea latex, purified and crystallized by the hanging-drop vapour-diffusion method. A data set was collected to 2.0 Å resolution in-house from a single crystal at 110 K. The crystals belonged to the trigonal space group P3121 or P3221, with unit-cell parameters a = b = 126.9, c = 84.6 Å, α = β = 90, γ = 120°. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient is 2.46 Å3 Da-1, corresponding to a solvent content of 50%. Structure determination of the enzyme is in progress.

Year: 2009
OAI identifier: oai:ub.rug.nl:dbi/4a11323ed0f73
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