@article {4772,
	title = {Structural proteomics of an archaeon},
	journal = {Nature Structural Biology},
	volume = {7},
	number = {10},
	year = {2000},
	note = {ISI Document Delivery No.: 362LRTimes Cited: 188Cited Reference Count: 29},
	month = {Oct},
	pages = {903-909},
	type = {Article},
	abstract = {A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, similar to 20\% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility. implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics},
	keywords = {ALIGNMENT, CLASSIFICATION, GENE, genomics, PREDICTION, PROTEIN-STRUCTURE, SCOP},
	isbn = {1072-8368},
	url = {<Go to ISI>://000089779900022},
	author = {Christendat, D. and Yee, A. and Dharamsi, A. and Kluger, Y. and Savchenko, A. and Cort, J. R. and Booth, V. and Mackereth, C. D. and Saridakis, V. and Ekiel, I. and Kozlov, G. and Maxwell, K. L. and Wu, N. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Davidson, A. R. and Pai, E. F. and Gerstein, M. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {4873,
	title = {Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {97},
	number = {12},
	year = {2000},
	note = {ISI Document Delivery No.: 322UATimes Cited: 14Cited Reference Count: 34},
	month = {Jun},
	pages = {6316-6321},
	type = {Article},
	abstract = {The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast, Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three cu-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX2CXnCC sequence motif and serves to bridge an N-terminal loop with helix 3, This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.},
	keywords = {ABC10-BETA, ARCHAEA, COMMON SUBUNITS, DOMAIN, genomics, IN-VITRO, PROTEINS, RESOLUTION, SEQUENCE, transcription},
	isbn = {0027-8424},
	url = {<Go to ISI>://000087526300018},
	author = {Mackereth, C. D. and Arrowsmith, C. H. and Edwards, A. M. and McIntosh, L. P.}
}
