A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum

Santosh Panjikar; Lars Thomsen; Kane Michael O'Donnell; Alan Riboldi-Tunnicliffe

doi:10.1107/S1600576715006147

A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum

Santosh Panjikar
, Lars Thomsen
, Kane Michael O'Donnell
, Alan Riboldi-Tunnicliffe

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

2 Citations (Scopus)

Abstract

Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10^-5mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10^-5mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.

Original language	English
Pages (from-to)	913-916
Number of pages	4
Journal	Journal of Applied Crystallography
Volume	48
DOIs	https://doi.org/10.1107/S1600576715006147
Publication status	Published - 1 Jun 2015
Externally published	Yes

Keywords

long-wavelength crystallography
lysozyme
proteinase K
sulfur single-wavelength anomalous diffraction
vacuum

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10.1107/S1600576715006147

Cite this

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title = "A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum",

abstract = "Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10-5mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10-5mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.",

keywords = "long-wavelength crystallography, lysozyme, proteinase K, sulfur single-wavelength anomalous diffraction, vacuum",

author = "Santosh Panjikar and Lars Thomsen and O'Donnell, \{Kane Michael\} and Alan Riboldi-Tunnicliffe",

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T1 - A step towards long-wavelength protein crystallography

T2 - Subjecting protein crystals to a vacuum

AU - Panjikar, Santosh

AU - Thomsen, Lars

AU - O'Donnell, Kane Michael

AU - Riboldi-Tunnicliffe, Alan

PY - 2015/6/1

Y1 - 2015/6/1

N2 - Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10-5mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10-5mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.

AB - Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10-5mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10-5mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.

KW - long-wavelength crystallography

KW - lysozyme

KW - proteinase K

KW - sulfur single-wavelength anomalous diffraction

KW - vacuum

UR - https://www.scopus.com/pages/publications/84930628888

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DO - 10.1107/S1600576715006147

M3 - Article

AN - SCOPUS:84930628888

SN - 0021-8898

VL - 48

SP - 913

EP - 916

JO - Journal of Applied Crystallography

JF - Journal of Applied Crystallography

ER -

A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum

Abstract

Keywords

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