{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Koide S"],"funding":["NIDA NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["449-57"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2736338"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(4)"],"pubmed_abstract":["The preparation of diffraction quality crystals remains the major bottleneck in macromolecular X-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology."],"journal":["Current opinion in structural biology"],"pubmed_title":["Engineering of recombinant crystallization chaperones."],"pmcid":["PMC2736338"],"funding_grant_id":["R21 CA132700","U54-GM74946","R01 GM072688","R21 DA025725","U54 GM074946","R01-GM72688","R01 GM072688-01","U54 GM074946-010002","R21-CA132700","R21 DA025725-01","R21 CA132700-01","R21-DA025725"],"pubmed_authors":["Koide S"],"additional_accession":[]},"is_claimable":false,"name":"Engineering of recombinant crystallization chaperones.","description":"The preparation of diffraction quality crystals remains the major bottleneck in macromolecular X-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology.","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Aug","modification":"2024-10-16T11:09:41.819Z","creation":"2019-03-27T00:24:38Z"},"accession":"S-EPMC2736338","cross_references":{"pubmed":["19477632"],"doi":["10.1016/j.sbi.2009.04.008"]}}