PMCC PMCC

Search tips
Search criteria

Advanced
Results 1-3 (3)
 

Clipboard (0)
None

Select a Filter Below

Journals
Authors
Year of Publication
Document Types
1.  Crystallization and preliminary X-ray crystallographic analysis of the putative NADP(H)-dependent oxidoreductase YncB from Vibrio vulnificus  
In order to investigate its structure and function, the medium-chain dehydrogenase/reductase superfamily YncB-like protein from V. vulnificus was expressed, purified and crystallized. X-ray diffraction analyses of YncB and the YncB–NADP(H) complex are reported at resolutions of 1.85 and 1.81 Å, respectively.
The yncB gene product from Vibrio vulnificus, which belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily, was crystallized using the microbatch crystallization method at 295 K. Diffraction data sets were collected using synchrotron radiation. Crystals of selenomethionine-substituted YncB protein belonged to space group P212121, with unit-cell parameters a = 90.52, b = 91.56, c = 104.79 Å. Assuming the presence of two molecules in the asymmetric unit, the solvent content was estimated to be about 57%. Crystals of the YncB–NADP(H) complex belonged to space group P41212 or P43212, with unit-cell parameters a = b = 90.14, c = 105.61 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 56.42%.
doi:10.1107/S1744309112030527
PMCID: PMC3433207  PMID: 22949204
MDR superfamily; Vibrio vulnificus; YncB
2.  In-House Zinc SAD Phasing at Cu Kα Edge 
Molecules and Cells  2013;36(1):74-81.
De novo zinc single-wavelength anomalous dispersion (Zn-SAD) phasing has been demonstrated with the 1.9 Å resolution data of glucose isomerase and 2.6 Å resolution data of Staphylococcus aureus Fur (SaFur) collected using in-house Cu Kα X-ray source. The successful in-house Zn-SAD phasing of glucose isomerase, based on the anomalous signals of both zinc ions introduced to crystals by soaking and native sulfur atoms, drove us to determine the structure of SaFur, a zinc-containing transcription factor, by Zn-SAD phasing using in-house X-ray source. The abundance of zinc-containing proteins in nature, the easy zinc derivatization of the protein surface, no need of synchrotron access, and the successful experimental phasing with the modest 2.6 Å resolution SAD data indicate that in-house Zn-SAD phasing can be widely applicable to structure determination.
doi:10.1007/s10059-013-0074-1
PMCID: PMC3887929  PMID: 23686432
anomalous scattering; experimental phasing; protein crystallography; SAD phasing; zinc
3.  Experimental phasing using zinc anomalous scattering 
The surface of proteins can be charged with zinc ions and the anomalous signals from these zinc ions can be used for structure determination of proteins.
Zinc is a suitable metal for anomalous dispersion phasing methods in protein crystallography. Structure determination using zinc anomalous scattering has been almost exclusively limited to proteins with intrinsically bound zinc(s). Here, it is reported that multiple zinc ions can easily be charged onto the surface of proteins with no intrinsic zinc-binding site by using zinc-containing solutions. Zn derivatization of protein surfaces appears to be a largely unnoticed but promising method of protein structure determination.
doi:10.1107/S0907444912024420
PMCID: PMC3489106  PMID: 22948927
zinc anomalous scattering; phasing; Zn derivatization

Results 1-3 (3)