<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>67</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>68(Pt 1)</volume><submitter>Bunker RD</submitter><pubmed_abstract>Human dihydrodipicolinate synthase-like protein (DHDPSL) is a gene product of unknown function. It is homologous to bacterial pyruvate-dependent aldolases such as dihydrodipicolinate synthase (DHDPS), which functions in lysine biosynthesis. However, it cannot have this function and instead is implicated in a genetic disorder that leads to excessive production of oxalate and kidney-stone formation. In order to better understand its function, DHDPSL was expressed as an MBP-fusion protein and crystallized using an in situ proteolysis protocol. Two crystal forms were obtained, both of which diffracted X-rays to approximately 2.0 Å resolution. One of these, belonging to space group P6(2)22 or P6(4)22 with unit-cell parameters a = b = 142.9, c = 109.8 Å, ? = ? = 90, ? = 120°, was highly reproducible and suitable for structure determination by X-ray crystallography.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>59-62</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3253836</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Purification, crystallization and preliminary crystallographic analysis of human dihydrodipicolinate synthase-like protein (DHDPSL).</pubmed_title><pmcid>PMC3253836</pmcid><pubmed_authors>Bunker RD</pubmed_authors><pubmed_authors>Baker EN</pubmed_authors><pubmed_authors>Loomes KM</pubmed_authors><view_count>67</view_count></additional><is_claimable>false</is_claimable><name>Purification, crystallization and preliminary crystallographic analysis of human dihydrodipicolinate synthase-like protein (DHDPSL).</name><description>Human dihydrodipicolinate synthase-like protein (DHDPSL) is a gene product of unknown function. It is homologous to bacterial pyruvate-dependent aldolases such as dihydrodipicolinate synthase (DHDPS), which functions in lysine biosynthesis. However, it cannot have this function and instead is implicated in a genetic disorder that leads to excessive production of oxalate and kidney-stone formation. In order to better understand its function, DHDPSL was expressed as an MBP-fusion protein and crystallized using an in situ proteolysis protocol. Two crystal forms were obtained, both of which diffracted X-rays to approximately 2.0 Å resolution. One of these, belonging to space group P6(2)22 or P6(4)22 with unit-cell parameters a = b = 142.9, c = 109.8 Å, ? = ? = 90, ? = 120°, was highly reproducible and suitable for structure determination by X-ray crystallography.</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Jan</publication><modification>2021-02-19T18:47:46Z</modification><creation>2019-03-27T00:01:32Z</creation></dates><accession>S-EPMC3253836</accession><cross_references><pubmed>22232173</pubmed><doi>10.1107/s1744309111048068</doi><doi>10.1107/S1744309111048068</doi></cross_references></HashMap>