@article { ISI:000278165900028,
	title = {Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from thermus thermophilus},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {66},
	number = {6},
	year = {2010},
	month = {JUN},
	pages = {738-743},
	publisher = {WILEY-BLACKWELL PUBLISHING, INC},
	address = {COMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USA},
	abstract = {<p>The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg(2+) or Mn(2+) and with the help of NAD(+). In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt-IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported.</p>},
	issn = {1744-3091},
	doi = {10.1107/S174430911001626X},
	author = {Merli, Angelo and Manikandan, Karuppasamy and Graczer, Eva and Schuldt, Linda and Singh, Rajesh Kumar and Zavodszky, Peter and Vas, Maria and Weiss, Manfred S.}
}
