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Expression, purification, crystallization and crystallographic study of Lutzomyia longipalpis LJL143
Author(s) -
Kelleher Alan,
Liu Zhuyun,
Seid Christopher A.,
Zhan Bin,
Asojo Oluwatoyin A.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15009486
Subject(s) - sandfly , orthorhombic crystal system , crystallization , crystallography , molecular replacement , leishmaniasis , leishmania , lutzomyia , biology , veterinary medicine , chemistry , parasite hosting , crystal structure , immunology , psychodidae , medicine , organic chemistry , world wide web , computer science
Leishmaniasis is a neglected vector‐borne disease with a global prevalence of over 12 million cases and 59 000 annual deaths. Transmission of the parasite requires salivary proteins, including LJL143 from the New World sandfly Lutzomyia longipalpis . LJL143 is a known marker of sandfly exposure in zoonotic hosts. LJL143 was crystallized from soluble protein expressed using Pichia pastoris . X‐ray data were collected to 2.6 Å resolution from orthorhombic crystals belonging to space group P 2 1 2 1 2 1 , with average unit‐cell parameters a = 57.39, b = 70.24, c = 79.58 Å. The crystals are predicted to have a monomer in the asymmetric unit, with an estimated solvent content of 48.5%. LJL143 has negligible homology to any reported structures, so the phases could not be determined by molecular replacement. All attempts at S‐SAD failed and future studies include experimental phase determination using heavy‐atom derivatives.