Expression, purification, crystallization and preliminary X-ray diffraction studies of bacterial and archaeal L4 ribosomal proteins

Michael Worbs; Markus C. Wahl

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Expression, purification, crystallization and preliminary X-ray diffraction studies of bacterial and archaeal L4 ribosomal proteins

机译：表达,纯化,结晶初步的x射线衍射的研究细菌和古细菌L4核糖体蛋白质

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Ribosomal protein L4 is implicated in the peptidyltransferase activity of the ribosome and in certain bacteria it regulates the transcription and translation of the 11-gene S10 operon. The genes for the L4 ribosomal proteins from the hyperthermophilic bacterium Thermotoga maritima and the halophilic archaeon Haloarcula marismortui have been PCR amplified from genomic DNA and cloned under the control of a T7 promoter to generate overexpressing Escherichia coli strains. For both proteins, efficient purification procedures were developed to yield material suitable for crystallization trials. Crystals of T. maritima L4 were obtained in the orthorhombic space group P2_12_12_1, with one molecule per asymmetric unit, diffracting to 1.7 A resolution with synchrotron radiation. Crystals of H. marismortui L4 belonged to the trigonal space group P3_121 or P3_221 and diffracted to 3.2 A resolution with a rotating-anode source, presumably containing three molecules per asymmetric unit. The results demonstrate that for certain halophilic proteins the same purification and crystallization procedures can be employed as for conventional proteins.

机译：核糖体蛋白L4有牵连肽基转移酶活动的核糖体和在某些细菌它调节11-gene S10的转录和翻译操纵子。从hyperthermophilic细菌Thermotogamaritima和嗜盐的archaeon Haloarculamarismortui从基因组PCR扩增DNA和克隆一个T7启动子的控制下生成overexpressing大肠杆菌菌株。净化程序开发收益材料适合结晶试验。晶体的t . maritima L4得到的斜方晶系的空间群P2_12_12_1,分子/不对称单位,衍射到1.7与同步辐射分辨率。的h . marismortui L4属于三方空间群P3_121 P3_221和衍射3.2与旋转阳极来源一项决议,大概每包含三个分子不对称单元。某些嗜盐的蛋白质相同的净化可以使用和结晶过程传统蛋白质。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第5期|645-647|共3页
作者
Michael Worbs; Markus C. Wahl;
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Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany;

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正文语种英语
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Haloarcula marismortui; Purification; Thermotoga maritimaX-ray diffractionRibosomesgenomic DNARibosomal ProteinsPeptidyl TransferasesCrystallization;

机译：Haloarcula marismortui;净化;ThermotogamaritimaX-ray diffractionRibosomesgenomicTransferasesCrystallization;

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Expression, purification, crystallization and preliminary X-ray diffraction studies of bacterial and archaeal L4 ribosomal proteins

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