Literature summary for 1.1.1.B51 extracted from

Takeshita, D.; Kataoka, M.; Miyakawa, T.; Miyazono, K.; Uzura, A.; Nagata, K.; Shimizu, S.; Tanokura, M.
Crystallization and preliminary X-ray analysis of the NADPH-dependent 3-quinuclidinone reductase from Rhodotorula rubra (2009), Acta Crystallogr. Sect. F, 65, 645-647.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Rhodotorula mucilaginosa

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapour-diffusion method using PEG 8000 as the precipitant. The crystals belonged to space group P4(1)2(1)2, with unit-cell parameters a = b = 91.3, c = 265.4 A, and diffracted X-rays to 2.2 A resolution.The asymmetric unit contained four molecules of the protein and the solvent content was 48.4%	Rhodotorula mucilaginosa

Organism

Organism	UniProt	Comment	Textmining
Rhodotorula mucilaginosa	B9ZZZ6	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-affinity and ion-exchange column chromatography	Rhodotorula mucilaginosa

Subunits

Subunits	Comment	Organism
tetramer	crystallographic data	Rhodotorula mucilaginosa

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Release 2023.1 (January 2023)