Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea

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Standard

Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea. / Skov, L K; Mirza, Osman Asghar; Henriksen, A; Potocki de Montalk, G; Remaud-Simeon, M; Sarcabal, P; Willemot, R M; Monsan, P; Gajhede, M.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 56, No. Pt 2, 02.2000, p. 203-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Skov, LK, Mirza, OA, Henriksen, A, Potocki de Montalk, G, Remaud-Simeon, M, Sarcabal, P, Willemot, RM, Monsan, P & Gajhede, M 2000, 'Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea', Acta Crystallographica. Section D: Biological Crystallography, vol. 56, no. Pt 2, pp. 203-5.

APA

Skov, L. K., Mirza, O. A., Henriksen, A., Potocki de Montalk, G., Remaud-Simeon, M., Sarcabal, P., Willemot, R. M., Monsan, P., & Gajhede, M. (2000). Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea. Acta Crystallographica. Section D: Biological Crystallography, 56(Pt 2), 203-5.

Vancouver

Skov LK, Mirza OA, Henriksen A, Potocki de Montalk G, Remaud-Simeon M, Sarcabal P et al. Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea. Acta Crystallographica. Section D: Biological Crystallography. 2000 Feb;56(Pt 2):203-5.

Author

Skov, L K ; Mirza, Osman Asghar ; Henriksen, A ; Potocki de Montalk, G ; Remaud-Simeon, M ; Sarcabal, P ; Willemot, R M ; Monsan, P ; Gajhede, M. / Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea. In: Acta Crystallographica. Section D: Biological Crystallography. 2000 ; Vol. 56, No. Pt 2. pp. 203-5.

Bibtex

@article{41e8664c3970469bbb5f77a725d3b56f,

title = "Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea",

abstract = "Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.",

keywords = "Bacterial Proteins, Circular Dichroism, Crystallization, Crystallography, X-Ray, Escherichia coli, Glucosyltransferases, Neisseria, Recombinant Proteins",

author = "Skov, {L K} and Mirza, {Osman Asghar} and A Henriksen and {Potocki de Montalk}, G and M Remaud-Simeon and P Sarcabal and Willemot, {R M} and P Monsan and M Gajhede",

year = "2000",

month = feb,

language = "English",

volume = "56",

pages = "203--5",

journal = "Acta Crystallographica Section D: Structural Biology",

issn = "2059-7983",

publisher = "International Union of Crystallography",

number = "Pt 2",

}

RIS

TY - JOUR

T1 - Crystallization and preliminary X-ray studies of recombinant amylosucrase from Neisseria polysaccharea

AU - Skov, L K

AU - Mirza, Osman Asghar

AU - Henriksen, A

AU - Potocki de Montalk, G

AU - Remaud-Simeon, M

AU - Sarcabal, P

AU - Willemot, R M

AU - Monsan, P

AU - Gajhede, M

PY - 2000/2

Y1 - 2000/2

N2 - Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.

AB - Recombinant amylosucrase from Neisseria polysaccharea was crystallized by the vapour-diffusion procedure in the presence of polyethylene glycol 6000. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 95.7, b = 117.2, c = 62.1 A, and diffract to 1.6 A resolution. A p-chloromercuribenzene sulfonate (pcmbs) derivative has been identified and a selenomethionine-substituted protein has been produced and crystallized.

KW - Bacterial Proteins

KW - Circular Dichroism

KW - Crystallization

KW - Crystallography, X-Ray

KW - Escherichia coli

KW - Glucosyltransferases

KW - Neisseria

KW - Recombinant Proteins

M3 - Journal article

VL - 56

SP - 203

EP - 205

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - Pt 2

ER -

ID: 47295081