Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin

Goedele Roos; Elke Brosens; Khadija Wahni; Aline Desmyter; Silvia Spinelli; Lode Wyns; Joris Messens; Remy Loris

doi:10.1107/S1744309106047075

Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin

Goedele Roos, Elke Brosens, Khadija Wahni, Aline Desmyter, Silvia Spinelli, Lode Wyns, Joris Messens, Remy Loris

Research output: Contribution to journal › Article › peer-review

Abstract

The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P2(1)2(1)2(1), with unit-cell parameters a = 41.7, b = 49.5, c = 55.6 A. The crystals diffract to 2.2 A resolution. Isomorphous crystals of wild-type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. These results suggest seeding as a valuable tool complementing surface engineering for proteins that are hard to crystallize.

Original language	English
Pages (from-to)	1255-1258
Number of pages	4
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	62
Issue number	Pt 12
DOIs	https://doi.org/10.1107/S1744309106047075
Publication status	Published - 1 Dec 2006

Keywords

Crystallization
Crystallography, X-Ray
Mutagenesis, Site-Directed
Staphylococcus aureus
Thioredoxins
Journal Article
Research Support, Non-U.S. Gov't

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Roos, G., Brosens, E., Wahni, K., Desmyter, A., Spinelli, S., Wyns, L., Messens, J., & Loris, R. (2006). Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(Pt 12), 1255-1258. https://doi.org/10.1107/S1744309106047075

Roos, Goedele ; Brosens, Elke ; Wahni, Khadija ; Desmyter, Aline ; Spinelli, Silvia ; Wyns, Lode ; Messens, Joris ; Loris, Remy. / Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins : the case of Staphylococcus aureus thioredoxin. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 ; Vol. 62, No. Pt 12. pp. 1255-1258.

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abstract = "The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P2(1)2(1)2(1), with unit-cell parameters a = 41.7, b = 49.5, c = 55.6 A. The crystals diffract to 2.2 A resolution. Isomorphous crystals of wild-type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. These results suggest seeding as a valuable tool complementing surface engineering for proteins that are hard to crystallize.",

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Roos, G, Brosens, E , Wahni, K, Desmyter, A, Spinelli, S, Wyns, L , Messens, J & Loris, R 2006, 'Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. Pt 12, pp. 1255-1258. https://doi.org/10.1107/S1744309106047075

Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins : the case of Staphylococcus aureus thioredoxin. / Roos, Goedele; Brosens, Elke ; Wahni, Khadija; Desmyter, Aline; Spinelli, Silvia; Wyns, Lode ; Messens, Joris ; Loris, Remy.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. Pt 12, 01.12.2006, p. 1255-1258.

Research output: Contribution to journal › Article › peer-review

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AU - Desmyter, Aline

AU - Spinelli, Silvia

AU - Wyns, Lode

AU - Messens, Joris

AU - Loris, Remy

PY - 2006/12/1

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N2 - The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P2(1)2(1)2(1), with unit-cell parameters a = 41.7, b = 49.5, c = 55.6 A. The crystals diffract to 2.2 A resolution. Isomorphous crystals of wild-type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. These results suggest seeding as a valuable tool complementing surface engineering for proteins that are hard to crystallize.

AB - The P31T mutant of Staphylococcus aureus thioredoxin crystallizes spontaneously in space group P2(1)2(1)2(1), with unit-cell parameters a = 41.7, b = 49.5, c = 55.6 A. The crystals diffract to 2.2 A resolution. Isomorphous crystals of wild-type thioredoxin as well as of other point mutants only grow when seeded with the P31T mutant. These results suggest seeding as a valuable tool complementing surface engineering for proteins that are hard to crystallize.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Mutagenesis, Site-Directed

KW - Staphylococcus aureus

KW - Thioredoxins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

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SN - 1744-3091

IS - Pt 12

ER -

Roos G, Brosens E , Wahni K, Desmyter A, Spinelli S, Wyns L et al. Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 Dec 1;62(Pt 12):1255-1258. https://doi.org/10.1107/S1744309106047075

Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin

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Keywords

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