A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction

2010 ◽  
Vol 66 (7) ◽  
pp. 762-769 ◽  
Author(s):  
Guillaume Pompidor ◽  
Olivier Maury ◽  
Jean Vicat ◽  
Richard Kahn

Tris-dipicolinate lanthanide complexes were used to prepare derivative crystals of six proteins: hen egg-white lysozyme, turkey egg-white lysozyme, thaumatin fromThaumatococcus daniellii, urate oxidase fromAspergillus flavus, porcine pancreatic elastase and xylanase fromTrichoderma reesei. Diffraction data were collected using either synchrotron radiation or X-rays from a laboratory source. In all cases, the complex turned out to be bound to the protein and the phases determined using the anomalous scattering of the lanthanide led to high-quality electron-density maps. The binding mode of the complex was characterized from the refined structures. The lanthanide tris-dipicolinate was found to bind through interactions between carboxylate groups of the dipicolinate ligands and hydrogen-bond donor groups of the protein. In each binding site, one enantiomeric form of the complex is selected from the racemic solution according to the specific site topology. For hen egg-white lysozyme and xylanase, derivative crystals obtained by cocrystallization belonged to a new monoclinicC2 crystal form that diffracted to high resolution.

1999 ◽  
Vol 55 (4) ◽  
pp. 745-752 ◽  
Author(s):  
Jun Dong ◽  
Titus J. Boggon ◽  
Naomi E. Chayen ◽  
James Raftery ◽  
Ru-Chang Bi ◽  
...  

A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air–liquid phase boundary, growth in gels and growth under oil (`microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid–liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid–gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 Å. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid–liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.


1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu

Sign in / Sign up

Export Citation Format

Share Document