Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)

(S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensi...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1996-07, Vol.52 (4), p.887-889
Hauptverfasser: Lauble, H., Knödler, S., Schindelin, H., Förster, S., Wajant, H., Effenberger, F.
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container_title Acta crystallographica. Section D, Biological crystallography.
container_volume 52
creator Lauble, H.
Knödler, S.
Schindelin, H.
Förster, S.
Wajant, H.
Effenberger, F.
description (S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensions are a = 71.4, b = 95.8, c = 149.1 Å. A complete set of diffraction data has been collected to 2.6 Å resolution. Form II crystals are grown from 500 mM Li2SO4 in 13% polyethylene glycol 8000. These crystals appear as hexagonal plates and diffract to 2.98 Å resolution but apparently are twinned. Cocrystallizing hydroxynitrile lyase with the inhibitor benzoic acid using 1.4 M (NH4)2SO4 in 100 mM Na citrate, pH 5.4 as precipitant yields crystal form III, which belongs to the monoclinic space group C2 with a = 150.7, b = 103.7, c = 90.6 Å, β = 101.3. X‐ray diffraction data were collected to 2.3 Å resolution.
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Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lauble, H.</au><au>Knödler, S.</au><au>Schindelin, H.</au><au>Förster, S.</au><au>Wajant, H.</au><au>Effenberger, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>1996-07</date><risdate>1996</risdate><volume>52</volume><issue>4</issue><spage>887</spage><epage>889</epage><pages>887-889</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>(S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. 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title Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)
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