干酪乳杆菌BL23肌醇脱氢酶LcIDH2的纯化、结晶及室温X射线衍射
Purification, crystallization and room-temperature X-ray diffraction of inositol dehydrogenase LcIDH2 from Lactobacillus casei BL23.
作者信息
Bertwistle Drew, Vogt Linda, Aamudalapalli Hari Babu, Palmer David R J, Sanders David A R
机构信息
Department of Chemistry, University of Saskatchewan, 110 Science Place, Saskatoon SK S7N 5C9, Canada.
出版信息
Acta Crystallogr F Struct Biol Commun. 2014 Jul;70(Pt 7):979-83. doi: 10.1107/S2053230X14011595. Epub 2014 Jun 19.
Abstract
Lactobacillus casei BL23 contains two genes, iolG1 and iolG2, homologous with inositol dehydrogenase encoding genes from many bacteria. Inositol dehydrogenase catalyzes the oxidation of inositol with concomitant reduction of NAD+. The protein encoded by iolG2, LcIDH2, has been purified to homogeneity, crystallized and cryoprotected for diffraction at 77 K. The crystals had a high mosaicity and poor processing statistics. Subsequent diffraction measurements were performed without cryoprotectant at room temperature. These crystals were radiation-resistant and a full diffraction data set was collected at room temperature to 1.6 Å resolution.
摘要
干酪乳杆菌BL23含有两个基因，iolG1和iolG2，它们与许多细菌中编码肌醇脱氢酶的基因同源。肌醇脱氢酶催化肌醇的氧化，并伴随NAD+的还原。由iolG2编码的蛋白质LcIDH2已被纯化至同质，结晶并进行了低温保护，以便在77 K下进行衍射。这些晶体具有高镶嵌性和较差的处理统计数据。随后在室温下无低温保护剂的情况下进行衍射测量。这些晶体具有抗辐射性，并在室温下收集了完整的衍射数据集，分辨率达到1.6 Å。
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