01534nas a2200229   4500008004100000022001400041245016000055210006900215260009200284300001200376490000700388520061800395100001801013700002801031700001701059700001901076700002501095700002101120700001501141700002301156856012501179       2010                        eng d  a1744-309100aCrystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from thermus thermophilus0 aCrystallization and preliminary Xray diffraction analysis of var  aCOMMERCE PLACE, 350 MAIN ST, MALDEN 02148, MA USAbWILEY-BLACKWELL PUBLISHING, INCcJUN  a738-7430 v663 a<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>1 aMerli, Angelo1 aManikandan, Karuppasamy1 aGraczer, Eva1 aSchuldt, Linda1 aSingh, Rajesh, Kumar1 aZavodszky, Peter1 aVas, Maria1 aWeiss, Manfred, S.  uhttps://library.ncl.res.in/content/crystallization-and-preliminary-x-ray-diffraction-analysis-various-enzyme-substrate-0