@article {5412,
	title = {Purification, characterization and crystallization of pyrroline-5-carboxylate reductase from the hyperthermophilic archeon Sulfolobus Solfataricus.},
	journal = {Protein Expression and Purification},
	volume = {64},
	year = {2009},
	month = {2009 Apr},
	pages = {125-30},
	abstract = {<p>The gene SSO0495 (proC), which encodes pyrroline-5-carboxylate reductase (P5CR) from the thermoacidophilic archeon Sulfolobus solfataricus P2 (Ss-P5CR), was cloned and expressed. The purified recombinant enzyme catalyzes the thioproline dehydrogenase with concomitant oxidation of NAD(P)H to NAD(P)+. This archeal enzyme has an optimal alkaline pH in this reversible reaction and is thermostable with a half-life of approximately 30 min at 80 degrees C. At pH 9.0, the reverse activation rate is nearly 3-fold higher than at pH 7.0. The homopolymer was characterized by cross-linking and size exclusion gel filtration chromatography. Ss-P5CR was crystallized by the hanging-drop vapor-diffusion method at 37 degrees C. Diffraction data were obtained to a resolution of 3.5A and were suitable for X-ray structure determination.</p>
},
	keywords = {Archaeal Proteins, Chromatography, Crystallization, Crystallography, Gel, Kinetics, NADP, Pyrroline Carboxylate Reductases, Sulfolobus solfataricus, Temperature, Thiazolidines, X-Ray},
	issn = {1096-0279},
	doi = {10.1016/j.pep.2008.10.018},
	author = {Meng, Zhaohui and Liu, Zhe and Lou, Zhiyong and Gong, Xiaocui and Cao, Yi and Bartlam, Mark and Zhang, Keqin and Rao, Zihe}
}
