Kim Hyun, Park Ae Kyung, Lee Jun Hyuck, Shin Seung Chul, Park Hyun, Kim Han Woo
Unit of Polar Genomics, Korea Polar Research Institute, Incheon 21990, Republic of Korea.
Acta Crystallogr F Struct Biol Commun. 2018 Jun 1;74(Pt 6):367-372. doi: 10.1107/S2053230X18007525. Epub 2018 May 31.
Esterases are very useful biocatalysts in industry: they hydrolyze esters and split them into a carboxylic acid and an alcohol. The psychrophilic esterase PsEst3 was obtained from Paenibacillus sp. R4, which was isolated from the active layer of the permafrost in Council, Alaska. PsEst3 was successfully overexpressed using a psychrophilic chaperonin co-expression system and was purified by nickel-affinity and size-exclusion chromatography. Recombinant PsEst3 was crystallized at 290 K using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.1 Å resolution. The crystal was determined to belong to space group P432 or P432, with unit-cell parameters a = b = c = 145.33 Å. Further crystallographic analysis needs to be conducted to investigate the structure and function of this esterase.
它们水解酯类,将其分解为羧酸和醇。嗜冷酯酶PsEst3是从芽孢杆菌属R4菌株中获得的,该菌株是从阿拉斯加康瑟尔的永久冻土活性层中分离出来的。使用嗜冷伴侣蛋白共表达系统成功地对PsEst3进行了过表达,并通过镍亲和色谱和尺寸排阻色谱进行了纯化。重组PsEst3采用悬滴气相扩散法在290 K下结晶。收集到了分辨率为2.1 Å的X射线衍射数据。该晶体被确定属于空间群P432或P432,晶胞参数a = b = c = 145.33 Å。需要进行进一步的晶体学分析来研究这种酯酶的结构和功能。