Open AccessCrystallization and preliminary X‐ray crystallographic analysis of a GroEL1 fragment from Mycobacterium tuberculosis H37Rv
Author(s) -
Sielaff Bernhard,
Lee Ki Seog,
Tsai Francis T. F.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110004409
Subject(s) - orthorhombic crystal system , mycobacterium tuberculosis , crystallization , crystallography , resolution (logic) , x ray crystallography , x ray , crystal structure , chemistry , diffraction , materials science , tuberculosis , physics , optics , medicine , pathology , organic chemistry , artificial intelligence , computer science
Full‐length GroEL1 from Mycobacterium tuberculosis H37Rv was cloned, overexpressed and purified. Crystals were obtained by the hanging‐drop vapor‐diffusion method and contained a 23 kDa GroEL1 fragment. A complete native data set was collected from a single frozen crystal that belonged to the orthorhombic space group P 2 1 2 1 2, with unit‐cell parameters a = 75.47, b = 78.67, c = 34.89 Å, α = β = γ = 90°, and diffracted to 2.2 Å resolution on a home X‐ray source.