Crystallization and preliminary crystallographic analysis of thermophilic cellulase from Fervidobacterium nodosum Rt17-B1.

ABSTRACT: FnCel5A, a thermostable endoglucanase, is a member of glycohydrolase family 5 which catalyzes the hydrolysis of cellulose to glucose in the thermophilic bacterium Fervidobacterium nodosum Rt17-B1. FnCel5A is particularly interesting because of its high thermostability (T(opt) = 353 K, half-life 48 h) and its high specific activity towards carboxymethylcellulose. These properties make FnCel5A an attractive target for protein engineering to improve cellulase activity. In order to resolve the crystal structure of FnCel5A and to gain a better understanding of its biological function, recombinant FnCel5A was expressed, purified and crystallized at 291 K using NaH(2)PO(4)/KH(2)PO(4) as a precipitant. A 2.4 A resolution native data set was collected from a single flash-cooled crystal (100 K) usin

SUBMITTER: Zheng B 

PROVIDER: S-EPMC2650467 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature