Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus

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Standard

Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. / Ernst, Heidi Asschenfeldt; Willemoës, Martin; Lo Leggio, Leila; Leonard, Gordon; Blum, Paul; Larsen, Sine.

I: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Bind 61, Nr. Pt 12, 2005, s. 1039-42.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Ernst, HA, Willemoës, M, Lo Leggio, L, Leonard, G, Blum, P & Larsen, S 2005, 'Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus', Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, bind 61, nr. Pt 12, s. 1039-42. https://doi.org/10.1107/S1744309105035177

APA

Ernst, H. A., Willemoës, M., Lo Leggio, L., Leonard, G., Blum, P., & Larsen, S. (2005). Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, 61(Pt 12), 1039-42. https://doi.org/10.1107/S1744309105035177

Vancouver

Ernst HA, Willemoës M, Lo Leggio L, Leonard G, Blum P, Larsen S. Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2005;61(Pt 12):1039-42. https://doi.org/10.1107/S1744309105035177

Author

Ernst, Heidi Asschenfeldt ; Willemoës, Martin ; Lo Leggio, Leila ; Leonard, Gordon ; Blum, Paul ; Larsen, Sine. / Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. I: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2005 ; Bind 61, Nr. Pt 12. s. 1039-42.

Bibtex

@article{1ed88cf06f8711de8bc9000ea68e967b,
title = "Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus",
abstract = "MalA is an alpha-glucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. It belongs to glycoside hydrolase family 31, which includes several medically interesting alpha-glucosidases. MalA and its selenomethionine derivative have been overproduced in Escherichia coli and crystallized in four different crystal forms. Microseeding was essential for the formation of good-quality crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets could be collected. The most suitable crystals for structure determination are the monoclinic form 4 crystals, belonging to space group P2(1), from which data sets extending to 2.5 A resolution have been collected. Self-rotation functions calculated for this form and for the orthorhombic (P2(1)2(1)2(1)) form 2 indicate the presence of six molecules in the asymmetric unit related by 32 symmetry.",
author = "Ernst, {Heidi Asschenfeldt} and Martin Willemo{\"e}s and {Lo Leggio}, Leila and Gordon Leonard and Paul Blum and Sine Larsen",
note = "Keywords: Carbohydrates; Crystallography, X-Ray; Escherichia coli; Maltose; Oligosaccharides; Plasmids; Protein Structure, Tertiary; Substrate Specificity; Sulfolobus solfataricus; alpha-Glucosidases",
year = "2005",
doi = "10.1107/S1744309105035177",
language = "English",
volume = "61",
pages = "1039--42",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "Pt 12",

}

RIS

TY - JOUR

T1 - Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus

AU - Ernst, Heidi Asschenfeldt

AU - Willemoës, Martin

AU - Lo Leggio, Leila

AU - Leonard, Gordon

AU - Blum, Paul

AU - Larsen, Sine

N1 - Keywords: Carbohydrates; Crystallography, X-Ray; Escherichia coli; Maltose; Oligosaccharides; Plasmids; Protein Structure, Tertiary; Substrate Specificity; Sulfolobus solfataricus; alpha-Glucosidases

PY - 2005

Y1 - 2005

N2 - MalA is an alpha-glucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. It belongs to glycoside hydrolase family 31, which includes several medically interesting alpha-glucosidases. MalA and its selenomethionine derivative have been overproduced in Escherichia coli and crystallized in four different crystal forms. Microseeding was essential for the formation of good-quality crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets could be collected. The most suitable crystals for structure determination are the monoclinic form 4 crystals, belonging to space group P2(1), from which data sets extending to 2.5 A resolution have been collected. Self-rotation functions calculated for this form and for the orthorhombic (P2(1)2(1)2(1)) form 2 indicate the presence of six molecules in the asymmetric unit related by 32 symmetry.

AB - MalA is an alpha-glucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus. It belongs to glycoside hydrolase family 31, which includes several medically interesting alpha-glucosidases. MalA and its selenomethionine derivative have been overproduced in Escherichia coli and crystallized in four different crystal forms. Microseeding was essential for the formation of good-quality crystals of forms 2 and 4. For three of the crystal forms (2, 3 and 4) full data sets could be collected. The most suitable crystals for structure determination are the monoclinic form 4 crystals, belonging to space group P2(1), from which data sets extending to 2.5 A resolution have been collected. Self-rotation functions calculated for this form and for the orthorhombic (P2(1)2(1)2(1)) form 2 indicate the presence of six molecules in the asymmetric unit related by 32 symmetry.

U2 - 10.1107/S1744309105035177

DO - 10.1107/S1744309105035177

M3 - Journal article

C2 - 16511229

VL - 61

SP - 1039

EP - 1042

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

SN - 2053-230X

IS - Pt 12

ER -

ID: 13132146