title: Experimental phasing using zinc anomalous scattering.
abstract: 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.
authors.affiliation: Marine Biotechnology Research Center, Korea Institute of Ocean Science and Technology, Ansan 426-744, Republic of Korea. chajung@kordi.re.kr
authors.forename: Sun-Shin
authors.initials: SS
authors.lastname: Cha
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: An
authors.forename: Chang-Sook
authors.initials: CS
authors.lastname: Jeong
authors.forename: Min-Kyu
authors.initials: MK
authors.lastname: Kim
authors.forename: Sung-Gyu
authors.initials: SG
authors.lastname: Lee
authors.forename: Kwang-Hoon
authors.initials: KH
authors.lastname: Lee
authors.forename: Byung-Ha
authors.initials: BH
authors.lastname: Oh
mesh_terms: D008958:Models, Molecular; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D011506:Proteins / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*
chemical_list: D011506:Proteins; D015032:Zinc