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

Heidi Asschenfeldt Ernst; Martin Willemoës; Leila Lo Leggio; Gordon Leonard; Paul Blum; Sine Larsen

doi:10.1107/S1744309105035177

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

Heidi Asschenfeldt Ernst, Martin Willemoës, Leila Lo Leggio, Gordon Leonard, Paul Blum, Sine Larsen

5 Citations (Scopus)

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.

Original language	English
Journal	Acta Crystallographica. Section F : Structural Biology and Crystallization Communications
Volume	61
Issue number	Pt 12
Pages (from-to)	1039-42
Number of pages	3
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S1744309105035177
Publication status	Published - 2005

Access to Document

10.1107/S1744309105035177

Cite this

Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus. / Ernst, Heidi Asschenfeldt; Willemoës, Martin ; Lo Leggio, Leila et al.

In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Vol. 61, No. Pt 12, 2005, p. 1039-42.

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

@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",

}

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

SN - 2053-230X

VL - 61

SP - 1039

EP - 1042

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - Pt 12

ER -

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

Abstract

Access to Document

Fingerprint

Cite this