{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Feeling-Taylor AR"],"funding":["NHLBI NIH HHS"],"pagination":["2621-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC1304680"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["87(4)"],"pubmed_abstract":["Crystallization of the mutated hemoglobin, HbC, which occurs inside red blood cells of patients expressing betaC-globin and exhibiting the homozygous CC and the heterozygous SC (in which two mutant beta-globins, S and C, are expressed) diseases, is a convenient model for processes underlying numerous condensation diseases. As a first step, we investigated the molecular-level mechanisms of crystallization of this protein from high-concentration phosphate buffer in its stable carbomonoxy form using high-resolution atomic force microscopy. We found that in conditions of equilibrium with the solution, the crystals' surface reconstructs into four-molecule-wide strands along the crystallographic a (or b) axis. However, the crystals do not grow by the alignment of such preformed strands. We found"],"journal":["Biophysical journal"],"pubmed_title":["Crystallization mechanisms of hemoglobin C in the R state."],"pmcid":["PMC1304680"],"funding_grant_id":["1F31HL09564-01","HL58038","HL3865","F31 HL009564"],"pubmed_authors":["Nagel RL","Vekilov PG","Feeling-Taylor AR","Petsev DN","Hirsch RE","Yau ST"],"additional_accession":[]},"is_claimable":false,"name":"Crystallization mechanisms of hemoglobin C in the R state.","description":"Crystallization of the mutated hemoglobin, HbC, which occurs inside red blood cells of patients expressing betaC-globin and exhibiting the homozygous CC and the heterozygous SC (in which two mutant beta-globins, S and C, are expressed) diseases, is a convenient model for processes underlying numerous condensation diseases. As a first step, we investigated the molecular-level mechanisms of crystallization of this protein from high-concentration phosphate buffer in its stable carbomonoxy form using high-resolution atomic force microscopy. We found that in conditions of equilibrium with the solution, the crystals' surface reconstructs into four-molecule-wide strands along the crystallographic a (or b) axis. However, the crystals do not grow by the alignment of such preformed strands. We found","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 Oct","modification":"2025-04-18T12:15:01.141Z","creation":"2019-03-26T23:52:10Z"},"accession":"S-EPMC1304680","cross_references":{"pubmed":["15454456"],"doi":["10.1529/biophysj.104.039743"]}}