Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

K Dolmer; Lasse Bohl Jenner; L Jacobsen; Gregers Rom Andersen; T J Koch; S Thirup; L Sottrup-Jensen; J Nyborg

Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

K Dolmer, Lasse Bohl Jenner, L Jacobsen, Gregers Rom Andersen, T J Koch, S Thirup, L Sottrup-Jensen, J Nyborg

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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Abstract

The receptor-binding domains (RBDs) of human and bovine alpha 2-macroglobulin (alpha 2M) have been isolated after limited proteolysis of methylamine-treated alpha 2M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RBD are very thin plates unsuited for data collection. However, crystals of RBD from bovine alpha 2M give diffraction patterns suitable for X-ray analysis, and a complete dataset with a maximum resolution of 2.3 A has been collected with synchrotron radiation at cryogenic temperature. The crystals belong to spacegroup P3(1)21 or P3(2)21 with cell parameters a = b = 106.8 A, c = 72.2 A.

Original language	English
Journal	FEBS Letters
Volume	372
Issue	1
Pages (from-to)	93-5
Number of pages	2
ISSN	0014-5793
Publication status	Published - 1995

Keywords

Amino Acid Sequence
Animals
Binding Sites
Cattle
Crystallization
Crystallography, X-Ray
Humans
LDL-Receptor Related Protein 1
Molecular Sequence Data
Peptide Fragments
Receptors, Immunologic
Receptors, LDL
Sequence Alignment
alpha-Macroglobulins

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title = "Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin",

abstract = "The receptor-binding domains (RBDs) of human and bovine alpha 2-macroglobulin (alpha 2M) have been isolated after limited proteolysis of methylamine-treated alpha 2M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RBD are very thin plates unsuited for data collection. However, crystals of RBD from bovine alpha 2M give diffraction patterns suitable for X-ray analysis, and a complete dataset with a maximum resolution of 2.3 A has been collected with synchrotron radiation at cryogenic temperature. The crystals belong to spacegroup P3(1)21 or P3(2)21 with cell parameters a = b = 106.8 A, c = 72.2 A.",

keywords = "Amino Acid Sequence, Animals, Binding Sites, Cattle, Crystallization, Crystallography, X-Ray, Humans, LDL-Receptor Related Protein 1, Molecular Sequence Data, Peptide Fragments, Receptors, Immunologic, Receptors, LDL, Sequence Alignment, alpha-Macroglobulins",

author = "K Dolmer and Jenner, {Lasse Bohl} and L Jacobsen and Andersen, {Gregers Rom} and Koch, {T J} and S Thirup and L Sottrup-Jensen and J Nyborg",

year = "1995",

language = "English",

volume = "372",

pages = "93--5",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley & Sons Inc.",

number = "1",

}

Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin. / Dolmer, K; Jenner, Lasse Bohl; Jacobsen, L et al.
In: FEBS Letters, Vol. 372, No. 1, 1995, p. 93-5.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

AU - Dolmer, K

AU - Jenner, Lasse Bohl

AU - Jacobsen, L

AU - Andersen, Gregers Rom

AU - Koch, T J

AU - Thirup, S

AU - Sottrup-Jensen, L

AU - Nyborg, J

PY - 1995

Y1 - 1995

N2 - The receptor-binding domains (RBDs) of human and bovine alpha 2-macroglobulin (alpha 2M) have been isolated after limited proteolysis of methylamine-treated alpha 2M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RBD are very thin plates unsuited for data collection. However, crystals of RBD from bovine alpha 2M give diffraction patterns suitable for X-ray analysis, and a complete dataset with a maximum resolution of 2.3 A has been collected with synchrotron radiation at cryogenic temperature. The crystals belong to spacegroup P3(1)21 or P3(2)21 with cell parameters a = b = 106.8 A, c = 72.2 A.

AB - The receptor-binding domains (RBDs) of human and bovine alpha 2-macroglobulin (alpha 2M) have been isolated after limited proteolysis of methylamine-treated alpha 2M with papain. Single crystals of the RBDs have been grown by vapour diffusion. Crystals of human RBD are very thin plates unsuited for data collection. However, crystals of RBD from bovine alpha 2M give diffraction patterns suitable for X-ray analysis, and a complete dataset with a maximum resolution of 2.3 A has been collected with synchrotron radiation at cryogenic temperature. The crystals belong to spacegroup P3(1)21 or P3(2)21 with cell parameters a = b = 106.8 A, c = 72.2 A.

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Cattle

KW - Crystallization

KW - Crystallography, X-Ray

KW - Humans

KW - LDL-Receptor Related Protein 1

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Receptors, Immunologic

KW - Receptors, LDL

KW - Sequence Alignment

KW - alpha-Macroglobulins

M3 - Journal article

C2 - 7556651

SN - 0014-5793

VL - 372

SP - 93

EP - 95

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

Abstract

Keywords

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