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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Molecules (Basel, Switzerland)

High-Throughput Crystallization Pipeline at the Crystallography Core Facility of the Institut Pasteur

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecules (Basel, Switzerland) - 05 Dec 2019

Weber P, Pissis C, Navaza R, Mechaly AE, Saul F, Alzari PM, Haouz A

Link to Pubmed [PMID] – 31817305

Molecules 2019 Dec;24(24)

The availability of whole-genome sequence data, made possible by significant advances in DNA sequencing technology, led to the emergence of structural genomics projects in the late 1990s. These projects not only significantly increased the number of 3D structures deposited in the Protein Data Bank in the last two decades, but also influenced present crystallographic strategies by introducing automation and high-throughput approaches in the structure-determination pipeline. Today, dedicated crystallization facilities, many of which are open to the general user community, routinely set up and track thousands of crystallization screening trials per day. Here, we review the current methods for high-throughput crystallization and procedures to obtain crystals suitable for X-ray diffraction studies, and we describe the crystallization pipeline implemented in the medium-scale crystallography platform at the Institut Pasteur (Paris) as an example.

https://www.ncbi.nlm.nih.gov/pubmed/31817305