<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Feeling-Taylor AR</submitter><funding>NHLBI NIH HHS</funding><pagination>2621-9</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC1304680</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>87(4)</volume><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</pubmed_abstract><journal>Biophysical journal</journal><pubmed_title>Crystallization mechanisms of hemoglobin C in the R state.</pubmed_title><pmcid>PMC1304680</pmcid><funding_grant_id>1F31HL09564-01</funding_grant_id><funding_grant_id>HL58038</funding_grant_id><funding_grant_id>HL3865</funding_grant_id><funding_grant_id>F31 HL009564</funding_grant_id><pubmed_authors>Nagel RL</pubmed_authors><pubmed_authors>Vekilov PG</pubmed_authors><pubmed_authors>Feeling-Taylor AR</pubmed_authors><pubmed_authors>Petsev DN</pubmed_authors><pubmed_authors>Hirsch RE</pubmed_authors><pubmed_authors>Yau ST</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystallization mechanisms of hemoglobin C in the R state.</name><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</description><dates><release>2004-01-01T00:00:00Z</release><publication>2004 Oct</publication><modification>2025-04-18T12:15:01.141Z</modification><creation>2019-03-26T23:52:10Z</creation></dates><accession>S-EPMC1304680</accession><cross_references><pubmed>15454456</pubmed><doi>10.1529/biophysj.104.039743</doi></cross_references></HashMap>