Work

Of problems and opportunities—How to treat and how to not treat crystallographic fragment screening data

Year: 2022

Type: article

Abstract: In their recent commentary in Protein Science, Jaskolski et al. analyzed three randomly picked diffraction data sets from fragment-screening group depositions from the PDB and, based on that, they claimed that such data are principally problematic. We demonstrate here that if such data are treated properly, none of the proclaimed criticisms persist.

Source: Protein Science

DOI: 10.1002/pro.4391

Authors: Manfred S. Weiss, Jan Wollenhaupt, Galen J. Correy, James S. Fraser, Andreas Heine, Gerhard Klebe, Tobias Krojer, Marjolein Thunissen, Nicholas M. Pearce

Institutions: Helmholtz-Zentrum Berlin für Materialien und Energie, University of California, San Francisco, Philipps University of Marburg, Lund University, MAX IV Laboratory, Vrije Universiteit Amsterdam

Language: English

Topic: Enzyme Structure and Function

Subfield: Structural Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,950

Funders: Diamond Light Source, Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Award: Revolutionising macromolecular crystal structure determination through routine multi-dataset analysis

OpenAlex ID: W4293535521

FWCI: 1.064

Cites: 17

Cited by: 13

Related to: 10