Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1
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Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1. / Kulahin, Nikolaj; Kasper, Christina; Gajhede, Michael; Berezin, Vladimir; Bock, Elisabeth; Kastrup, Jette Sandholm Jensen.
In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 60, No. Pt 3, 03.2004, p. 591-3.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1
AU - Kulahin, Nikolaj
AU - Kasper, Christina
AU - Gajhede, Michael
AU - Berezin, Vladimir
AU - Bock, Elisabeth
AU - Kastrup, Jette Sandholm Jensen
PY - 2004/3
Y1 - 2004/3
N2 - Recombinant proteins consisting of either the four or five amino-terminal immunoglobulin (Ig) modules of the rat neural cell-adhesion molecule NCAM or the whole extracellular part [six Ig and five fibronectin type III (F3) modules] of mouse L1 have been expressed in Drosophila S2 cells. The proteins have been purified and crystallized. The crystals of the recombinant protein containing the four amino-terminal Ig modules of NCAM diffract X-rays to approximately 4 A resolution and belong to space group P622 or P6(3)22, with unit-cell parameters a = b = 258.7, c = 182.4 A. No diffraction was observed for the other two protein constructs. This is a step towards determining the structure of multimodular constructs of cell-adhesion molecules that exhibit high structural flexibility.
AB - Recombinant proteins consisting of either the four or five amino-terminal immunoglobulin (Ig) modules of the rat neural cell-adhesion molecule NCAM or the whole extracellular part [six Ig and five fibronectin type III (F3) modules] of mouse L1 have been expressed in Drosophila S2 cells. The proteins have been purified and crystallized. The crystals of the recombinant protein containing the four amino-terminal Ig modules of NCAM diffract X-rays to approximately 4 A resolution and belong to space group P622 or P6(3)22, with unit-cell parameters a = b = 258.7, c = 182.4 A. No diffraction was observed for the other two protein constructs. This is a step towards determining the structure of multimodular constructs of cell-adhesion molecules that exhibit high structural flexibility.
KW - Animals
KW - Cell Line
KW - Crystallization
KW - Crystallography, X-Ray
KW - Drosophila
KW - Gene Expression
KW - Mice
KW - Neural Cell Adhesion Molecule L1
KW - Protein Structure, Tertiary
KW - Rats
KW - Recombinant Proteins
U2 - 10.1107/S0907444904001167
DO - 10.1107/S0907444904001167
M3 - Journal article
C2 - 14993704
VL - 60
SP - 591
EP - 593
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 2059-7983
IS - Pt 3
ER -
ID: 44729822