A fast and portable microspectrophotometer for protein crystallography

Hadfield, Andrea T.; Hajdu, János

doi:10.1107/s0021889893005552

Cited by 86 publications

(52 citation statements)

References 10 publications

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“…For such work, it is necessary that an investigator use a single-crystal microspectrophotometer with a millisecond time resolution, such as that described by Hadfield & Hajdu (1993). Such devices, while essential for singleturnover Laue experiments that capture diffraction information during the lifetime of an intermediate species during an initial synchronized catalytic cycle, cost a minimum of $20 000, up to approximately $150 000 for commerically available instrumentation.…”

Section: Resultsmentioning

confidence: 99%

Direct measurement of diffusion rates in enzyme crystals by video absorbance spectroscopy

Ohara¹,

Goodwin²,

Stoddard³

1995

J Appl Cryst

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In order to directly observe the structure of enzyme intermediate complexes that form during turnover, one must ensure the homogeneous and complete accumulation of the intermediate during the collection of diffraction data. In the case of * Author to whom all correspondence should be addressed.:~:~ 1995 International Union of Crystallography Printed in Great Britain -all rights reserved steady-state Laue experiments, the accumulation of the intermediate is dictated by the rate of substrate diffusion throughout the crystal, compared with the rate of turnover and disappearance of a rate-limited catalytic intermediate. This paper describes a simple quantitative method for measuring substrate diffusion and binding within an enzyme crystal. The set-up consists of a light source, specific bandpass filters, a crystallographic flow cell, a syringe pump, a charge-coupleddevice color video camera and a workstation with a frame- Journal of Applied Crystallography

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Section: Resultsmentioning

confidence: 99%

Direct measurement of diffusion rates in enzyme crystals by video absorbance spectroscopy

Ohara¹,

Goodwin²,

Stoddard³

1995

J Appl Cryst

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“…Spectra were generated from the integration of 10 19-ms exposures (33). Optimal diffraction data were collected from crystals too small for accurate spectral measurement by the microspectrophotometer.…”

Section: Methodsmentioning

confidence: 99%

Structural Snapshots from the Oxidative Half-reaction of a Copper Amine Oxidase

Johnson

Yukl

Klema

et al. 2013

Journal of Biological Chemistry

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Background: Copper amine oxidases activate O 2 either at the copper center or aminoquinol cofactor. Results: Catalytic intermediates from the oxidative half-reaction are structurally and spectroscopically characterized. Conclusion: The mechanism of O 2 activation may depend on accessibility dictated by two conformers of the quinone cofactor. Significance: Structural changes that inform on catalytic mechanism have been revealed in the ubiquitous copper amine oxidases.

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“…Safety precautions were taken to minimize the risk of fire and explosions with high-pressure oxygen. Ultraviolet spectra of single crystals were recorded as described 15 .…”

Section: Oxygenation Experimentsmentioning

confidence: 99%