Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae.
The potentially structured core domain of the intrinsically disordered protein Knr4 from Saccharomyces cerevisiae, comprising residues 80-340, was expressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method. Selenomethionine-containing (SeMet) protein was also purified and crystallized. Crystals of both proteins belonged to space group P6522, with unit-cell parameters a = b = 112.44, c = 265.21 Å for the native protein and a = b = 112.49, c = 262.21 Å for the SeMet protein, and diffracted to 3.50 and 3.60 Å resolution, respectively. There are two molecules in the asymmetric unit related by a twofold axis. The anomalous signal of selenium was recorded and yielded an electron-density map of sufficient quality to allow the identification of secondary-structure elements.
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Sylviane
S
Julien
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Patrick
P
Tondl
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077 Toulouse, France.
Fabien
F
Durand
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077 Toulouse, France.
Adilia
A
Dagkessamanskaia
Institut de Biologie Intégrative de la Cellule, UMR9198, CNRS-Université Paris Sud, Bâtiment 430, 91400 Orsay, France.
Herman
H
van Tilbeurgh
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077 Toulouse, France.
Jean Marie
JM
François
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Lionel
L
Mourey
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Didier
D
Zerbib
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077 Toulouse, France.
Hélène
H
Martin-Yken
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Laurent
L
Maveyraud
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D014157:Transcription Factors / Q000737:chemistry*; D014466:Ultraviolet Rays
D011994:Recombinant Proteins; C085451:SMI1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors
Saccharomyces cerevisiae; cell-wall biogenesis regulation; hub proteins; intrinsically disordered proteins