{
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      "official_url": "http:\/\/scripts.iucr.org\/cgi-bin\/paper?S1744309108002753",
      "keywords": "aspartate semialdehyde dehydrogenase; Mycobacterium tuberculosis; Rv3708c.",
      "pagerange": "167-70",
      "publisher": "International Union of Crystallography",
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      "publication": "Acta crystallographica. Section F, Structural biology and crystallization communications",
      "abstract": "Aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis (Asd, ASADH, Rv3708c), which is the second enzyme in the lysine\/homoserine-biosynthetic pathways, has been expressed heterologously in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Preliminary diffraction data analysis suggested the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form A and of one or two monomers in the cubic crystal form B.",
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      "title": "Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.",
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      "volume": 64,
      "note": "Copyright of this article belongs toInternational Union of Crystallography.",
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