5AMW

Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 2 protein (A141F) processed with the CrystalDirect automated mounting and cryo-cooling technology

Summary for 5AMW

• Entry DOI: 10.2210/pdb5amw/pdb
• Related: 5AMX 5AMY 5AMZ 5AN2 5AN4 5AND 5ANE 5ANG 5ANI 5ANJ 5ANK 5ANL 5ANO
• Descriptor: Fra a 2 allergen (2 entities in total)
• Functional Keywords: allergen, pyr/pyl/rcar, bet v 1, flavonoids, automated crystal harvesting, automated cryo-cooling, crystaldirect
• Biological source: Fragaria ananassa (Strawberry)
• Total number of polymer chains: 2
• Total formula weight: 35478.14

Authors

Zander, U.,Casanal, A.,Pott, D.,Valpuesta, V.,Hoffmann, G.,Cornaciu, I.,Cipriani, F.,Marquez, J.A. (deposition date: 2015-09-02, release date: 2016-04-13, Last modification date: 2024-05-08)

Primary citation

Zander, U.,Hoffmann, G.,Cornaciu, I.,Marquette, J.-P.,Papp, G.,Landret, C.,Seroul, G.,Sinoir, J.,Roewer, M.,Felisaz, F.,Rodriguez-Puente, S.,Mariaule, V.,Murphy, P.,Mathieu, M.,Cipriani, F.,Marquez, J.A.
Automated Harvesting and Processing of Protein Crystals Through Laser Photoablation.
Acta Crystallogr.,Sect.D, 72:454-, 2016

PubMed Abstract: Currently, macromolecular crystallography projects often require the use of highly automated facilities for crystallization and X-ray data collection. However, crystal harvesting and processing largely depend on manual operations. Here, a series of new methods are presented based on the use of a low X-ray-background film as a crystallization support and a photoablation laser that enable the automation of major operations required for the preparation of crystals for X-ray diffraction experiments. In this approach, the controlled removal of the mother liquor before crystal mounting simplifies the cryocooling process, in many cases eliminating the use of cryoprotectant agents, while crystal-soaking experiments are performed through diffusion, precluding the need for repeated sample-recovery and transfer operations. Moreover, the high-precision laser enables new mounting strategies that are not accessible through other methods. This approach bridges an important gap in automation and can contribute to expanding the capabilities of modern macromolecular crystallography facilities.

PubMed: 27050125
DOI: 10.1107/S2059798316000954

Experimental method

X-RAY DIFFRACTION (1.9 Å)