<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>51</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>65(Pt 5)</volume><submitter>Kernstock S</submitter><pubmed_abstract>Human ADP-ribosylhydrolase 1 (hARH1, ADPRH) cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein. hARH1 has been cloned, expressed heterologously in Escherichia coli, purified and crystallized in complex with K(+) and ADP. The orthorhombic crystals contained one monomer per asymmetric unit, exhibited a solvent content of 43% and diffracted X-rays to a resolution of 1.9 A. A prerequisite for obtaining well diffracting crystals was the performance of X-ray fluorescence analysis on poorly diffracting apo hARH1 crystals, which revealed the presence of trace amounts of K(+) in the crystal. Adding K-ADP to the crystallization cocktail then resulted in a crystal of different morphology and with dramatically improved diffraction properties.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>529-32</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2675603</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Cloning, expression, purification and crystallization as well as X-ray fluorescence and preliminary X-ray diffraction analyses of human ADP-ribosylhydrolase 1.</pubmed_title><pmcid>PMC2675603</pmcid><pubmed_authors>Mueller-Dieckmann J</pubmed_authors><pubmed_authors>Weiss MS</pubmed_authors><pubmed_authors>Mueller-Dieckmann C</pubmed_authors><pubmed_authors>Koch-Nolte F</pubmed_authors><pubmed_authors>Kernstock S</pubmed_authors><view_count>51</view_count></additional><is_claimable>false</is_claimable><name>Cloning, expression, purification and crystallization as well as X-ray fluorescence and preliminary X-ray diffraction analyses of human ADP-ribosylhydrolase 1.</name><description>Human ADP-ribosylhydrolase 1 (hARH1, ADPRH) cleaves the glycosidic bond of ADP-ribose attached to an Arg residue of a protein. hARH1 has been cloned, expressed heterologously in Escherichia coli, purified and crystallized in complex with K(+) and ADP. The orthorhombic crystals contained one monomer per asymmetric unit, exhibited a solvent content of 43% and diffracted X-rays to a resolution of 1.9 A. A prerequisite for obtaining well diffracting crystals was the performance of X-ray fluorescence analysis on poorly diffracting apo hARH1 crystals, which revealed the presence of trace amounts of K(+) in the crystal. Adding K-ADP to the crystallization cocktail then resulted in a crystal of different morphology and with dramatically improved diffraction properties.</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 May</publication><modification>2024-11-19T14:40:47.86Z</modification><creation>2019-03-26T22:31:52Z</creation></dates><accession>S-EPMC2675603</accession><cross_references><pubmed>19407395</pubmed><doi>10.1107/s1744309109014067</doi><doi>10.1107/S1744309109014067</doi></cross_references></HashMap>