Automated protein crystallization and a new crystal form of a subtilisin:eGlin complex

Henk A. Kelders; Kor H. Kalk; Piet Gros; Wim G.J. Hol

doi:10.1093/protein/1.4.301

Automated protein crystallization and a new crystal form of a subtilisin:eGlin complex

Henk A. Kelders^*, Kor H. Kalk, Piet Gros, Wim G.J. Hol

^*Corresponding author for this work

University of Groningen

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

Abstract

A procedure is described for automating labour-intensive steps of the 'hanging drop' protein crystallization method. An automatic sample changer is employed to fill the wells in a multi-well plate so that concentration gradients in various components are obtained. The sample changer is also used for preparing droplets on a second multi-well plate. Subse quently, this second plate is manually turned around and placed on top of the first multi-well plate such that a large number of chambers with different conditions is obtained simultaneously. During initial trials a new crystal form of a subtilisin:eglin complex was obtained. The crystals have space group P2₁ contain two enzyme inhibitor complexes per asymmetric unit and diffract beyond 2.2 Å.

Original language	English
Pages (from-to)	301-303
Number of pages	3
Journal	Protein Engineering, Design and Selection
Volume	1
Issue number	4
DOIs	https://doi.org/10.1093/protein/1.4.301
Publication status	Published - Aug 1987
Externally published	Yes

Bibliographical note

Funding Information:
It is a pleasure to acknowledge stimulating as well as critical discussions with Drs Jan Mctske van der Laan, Myra Swarte, Bauke Dijstra and Jan Dienth from the Groningen Protein Crystallography Group. This research was supported by Unilever, Vlaardingen, The Netherlands; Gist-Brocades, Delft, The Netherlands; the Groningen Protein Engineering Programme; and the Dutch Foundation of Chemical Research (SON) with financial aid from the Dutch Organisation for the Advancement of Pure Research (ZWO).

Funding

It is a pleasure to acknowledge stimulating as well as critical discussions with Drs Jan Mctske van der Laan, Myra Swarte, Bauke Dijstra and Jan Dienth from the Groningen Protein Crystallography Group. This research was supported by Unilever, Vlaardingen, The Netherlands; Gist-Brocades, Delft, The Netherlands; the Groningen Protein Engineering Programme; and the Dutch Foundation of Chemical Research (SON) with financial aid from the Dutch Organisation for the Advancement of Pure Research (ZWO).

Keywords

Automation
Crystallization
Subtilisin:eglin complex

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10.1093/protein/1.4.301

Cite this

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title = "Automated protein crystallization and a new crystal form of a subtilisin:eGlin complex",

abstract = "A procedure is described for automating labour-intensive steps of the 'hanging drop' protein crystallization method. An automatic sample changer is employed to fill the wells in a multi-well plate so that concentration gradients in various components are obtained. The sample changer is also used for preparing droplets on a second multi-well plate. Subse quently, this second plate is manually turned around and placed on top of the first multi-well plate such that a large number of chambers with different conditions is obtained simultaneously. During initial trials a new crystal form of a subtilisin:eglin complex was obtained. The crystals have space group P21 contain two enzyme inhibitor complexes per asymmetric unit and diffract beyond 2.2 {\AA}.",

keywords = "Automation, Crystallization, Subtilisin:eglin complex",

author = "Kelders, {Henk A.} and Kalk, {Kor H.} and Piet Gros and Hol, {Wim G.J.}",

note = "Funding Information: It is a pleasure to acknowledge stimulating as well as critical discussions with Drs Jan Mctske van der Laan, Myra Swarte, Bauke Dijstra and Jan Dienth from the Groningen Protein Crystallography Group. This research was supported by Unilever, Vlaardingen, The Netherlands; Gist-Brocades, Delft, The Netherlands; the Groningen Protein Engineering Programme; and the Dutch Foundation of Chemical Research (SON) with financial aid from the Dutch Organisation for the Advancement of Pure Research (ZWO).",

year = "1987",

month = aug,

doi = "10.1093/protein/1.4.301",

language = "English",

volume = "1",

pages = "301--303",

journal = "Protein Engineering, Design and Selection",

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publisher = "Oxford University Press",

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AU - Kelders, Henk A.

AU - Kalk, Kor H.

AU - Gros, Piet

AU - Hol, Wim G.J.

N1 - Funding Information: It is a pleasure to acknowledge stimulating as well as critical discussions with Drs Jan Mctske van der Laan, Myra Swarte, Bauke Dijstra and Jan Dienth from the Groningen Protein Crystallography Group. This research was supported by Unilever, Vlaardingen, The Netherlands; Gist-Brocades, Delft, The Netherlands; the Groningen Protein Engineering Programme; and the Dutch Foundation of Chemical Research (SON) with financial aid from the Dutch Organisation for the Advancement of Pure Research (ZWO).

PY - 1987/8

Y1 - 1987/8

N2 - A procedure is described for automating labour-intensive steps of the 'hanging drop' protein crystallization method. An automatic sample changer is employed to fill the wells in a multi-well plate so that concentration gradients in various components are obtained. The sample changer is also used for preparing droplets on a second multi-well plate. Subse quently, this second plate is manually turned around and placed on top of the first multi-well plate such that a large number of chambers with different conditions is obtained simultaneously. During initial trials a new crystal form of a subtilisin:eglin complex was obtained. The crystals have space group P21 contain two enzyme inhibitor complexes per asymmetric unit and diffract beyond 2.2 Å.

AB - A procedure is described for automating labour-intensive steps of the 'hanging drop' protein crystallization method. An automatic sample changer is employed to fill the wells in a multi-well plate so that concentration gradients in various components are obtained. The sample changer is also used for preparing droplets on a second multi-well plate. Subse quently, this second plate is manually turned around and placed on top of the first multi-well plate such that a large number of chambers with different conditions is obtained simultaneously. During initial trials a new crystal form of a subtilisin:eglin complex was obtained. The crystals have space group P21 contain two enzyme inhibitor complexes per asymmetric unit and diffract beyond 2.2 Å.

KW - Automation

KW - Crystallization

KW - Subtilisin:eglin complex

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DO - 10.1093/protein/1.4.301

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ER -

Automated protein crystallization and a new crystal form of a subtilisin:eGlin complex

Abstract

Bibliographical note

Funding

Keywords

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