» Articles » PMID: 30950396

How Best to Use Photons

Overview
Specialty Biochemistry
Date 2019 Apr 6
PMID 30950396
Citations 14
Authors
Affiliations
Soon will be listed here.
Abstract

Strategies for collecting X-ray diffraction data have evolved alongside beamline hardware and detector developments. The traditional approaches for diffraction data collection have emphasised collecting data from noisy integrating detectors (i.e. film, image plates and CCD detectors). With fast pixel array detectors on stable beamlines, the limiting factor becomes the sample lifetime, and the question becomes one of how to expend the photons that your sample can diffract, i.e. as a smaller number of stronger measurements or a larger number of weaker data. This parameter space is explored via experiment and synthetic data treatment and advice is derived on how best to use the equipment on a modern beamline. Suggestions are also made on how to acquire data in a conservative manner if very little is known about the sample lifetime.

Citing Articles

Useful experimental aspects of small-wedge synchrotron crystallography for accurate structure analysis of protein molecules.

Hirata K Acta Crystallogr D Struct Biol. 2024; 81(Pt 1):22-37.

PMID: 39718396 PMC: 11740584. DOI: 10.1107/S2059798324011987.


VMXm - A sub-micron focus macromolecular crystallography beamline at Diamond Light Source.

Warren A, Trincao J, Crawshaw A, Beale E, Duller G, Stallwood A J Synchrotron Radiat. 2024; 31(Pt 6):1593-1608.

PMID: 39475835 PMC: 11542661. DOI: 10.1107/S1600577524009160.


Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals.

Huang C, Aumonier S, Olieric V, Wang M Acta Crystallogr D Struct Biol. 2024; 80(Pt 8):620-628.

PMID: 39052318 PMC: 11301757. DOI: 10.1107/S2059798324006697.


Scaling and merging macromolecular diffuse scattering with mdx2.

Meisburger S, Ando N Acta Crystallogr D Struct Biol. 2024; 80(Pt 5):299-313.

PMID: 38606664 PMC: 11066883. DOI: 10.1107/S2059798324002705.


Scaling and merging macromolecular diffuse scattering with .

Meisburger S, Ando N bioRxiv. 2024; .

PMID: 38293202 PMC: 10827198. DOI: 10.1101/2024.01.16.575887.


References
1.
Diederichs K . Some aspects of quantitative analysis and correction of radiation damage. Acta Crystallogr D Biol Crystallogr. 2005; 62(Pt 1):96-101. DOI: 10.1107/S0907444905031537. View

2.
Waterman D, Winter G, Gildea R, Parkhurst J, Brewster A, Sauter N . Diffraction-geometry refinement in the DIALS framework. Acta Crystallogr D Struct Biol. 2016; 72(Pt 4):558-75. PMC: 4822564. DOI: 10.1107/S2059798316002187. View

3.
Yamamoto M, Hirata K, Yamashita K, Hasegawa K, Ueno G, Ago H . Protein microcrystallography using synchrotron radiation. IUCrJ. 2017; 4(Pt 5):529-539. PMC: 5619846. DOI: 10.1107/S2052252517008193. View

4.
Liu Q, Zhang Z, Hendrickson W . Multi-crystal anomalous diffraction for low-resolution macromolecular phasing. Acta Crystallogr D Biol Crystallogr. 2011; 67(Pt 1):45-59. PMC: 3016016. DOI: 10.1107/S0907444910046573. View

5.
Thorn A, Sheldrick G . ANODE: anomalous and heavy-atom density calculation. J Appl Crystallogr. 2012; 44(Pt 6):1285-1287. PMC: 3246834. DOI: 10.1107/S0021889811041768. View