@article { ISI:000236470000018,
	title = {Crystallization and preliminary X-ray characterization of a thermostable low-molecular-weight 1,4-beta-D-glucan glucohydrolase from an alkalothermophilic thermomonospora sp.},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {62},
	number = {4},
	year = {2006},
	month = {APR},
	pages = {385-387},
	publisher = {BLACKWELL PUBLISHING},
	type = {Article},
	address = {9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND},
	abstract = {<p>{Cellulases catalyze the hydrolysis of beta-1,4-glycosidic linkages within cellulose, the most abundant organic polymer on earth. The cellulase (TSC; EC 3.2.1.4) from an alkalothermophilic Thermomonospora sp. has a low molecular weight of 14.2 kDa. It is optimally active at 323 K and stable over the wide pH range of 5 - 9. Moreover, it has bifunctional activity against cellulose and xylan polymers. In this study, TSC was purified from the native source and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 49.9</p>},
	issn = {1744-3091},
	doi = {10.1107/S1744309106007949},
	author = {Manikandan, K. and Jagtap, Sharmili and Rao, M. and Ramakumar, S.}
}
@article { ISI:000241506400143,
	title = {Intact cell MALDI mass spectrometry as a tool to screen drugs in vivo for regulation of protein expression},
	journal = {Molecular \& Cellular Proteomics},
	volume = {5},
	number = {10, S},
	year = {2006},
	month = {OCT},
	pages = {S62},
	publisher = {AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC},
	type = {Meeting Abstract},
	address = {9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA},
	issn = {1535-9476},
	author = {Kulkarni, Mahesh J. and Vinod, V. P. and Umashankar, P. K. and Patole, M. and Rao, M.}
}
