Evidence map›Paper›PMID 21206046›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011

Crystallization and preliminary X-ray diffraction analysis of L,L-diaminopimelate aminotransferase (DapL) from Chlamydomonas reinhardtii.

André O Hudson, Irma Girón, Renwick C J Dobson

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
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1 · What the graph read from it

What it found

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

André O HudsonSchool of Biological and Medical Sciences, Rochester Institute of Technology, 85 Lomb Memorial Drive, Rochester, NY 14623-5603, USA.
Irma Girón
Renwick C J Dobson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the anabolic synthesis of diaminopimelate and lysine in plants and in some bacteria, the enzyme L,L-diaminopimelate aminotransferase (DapL; EC 2.6.1.83) catalyzes the conversion of tetrahydrodipicolinic acid (THDPA) to L,L-diaminopimelate, bypassing the DapD, DapC and DapE enzymatic steps in the bacterial acyl pathways. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapL from the alga Chlamydomonas reinhardtii are presented. Protein crystals were grown in conditions containing 25% (w/v) PEG 3350 and 200 mM lithium sulfate and initially diffracted to ∼1.35 Å resolution. They belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=58.9, b=91.8, c=162.9 Å. The data were processed to 1.55 Å resolution with an Rmerge of 0.081, an Rp.i.m. of 0.044, an Rr.i.m of 0.093 and a VM of 2.28 Å3 Da(-1).

Indexed as

Chlamydomonas reinhardtiiCloning, MolecularCrystallizationCrystallography, X-RayDiaminopimelic AcidMolecular Sequence DataMolecular StructurePlant ProteinsTransaminasesDiaminopimelic AcidPlant ProteinsTransaminases

Identifiers

PMID21206046
PMCPMC3079994

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