Search: onr:"swepub:oai:lup.lub.lu.se:c238e3cd-fee7-4423-9957-22abb966575e" > Crystallization and...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 03029naa a2200313 4500 | |
001 | oai:lup.lub.lu.se:c238e3cd-fee7-4423-9957-22abb966575e | |
003 | SwePub | |
008 | 160401s2003 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/1290652 URI |
024 | 7 | a https://doi.org/10.1107/S09074449020207472 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Bakhtiar, Shahrzadu Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-sba |
245 | 1 0 | a Crystallization and preliminary X-ray analysis of an alkaline serine protease from Nesterenkonia sp. Acta |
264 | 1 | c 2003 |
520 | a A novel calcium-independent serine protease from an alkaliphilic bacterium, Nesterenkonia sp. AL20, has been purified and crystallized at 296 K using sodium formate as the main precipitant. This enzyme is optimally active at pH 10, exhibits high stability towards autolytic digestion and its stability is not affected by the presence of EDTA or detergents. The triangular prism-shaped crystals diffracted X-rays to beyond 1.5 Å at a synchrotron beamline, with space group R3 and unit-cell parameters a = b = 92.26, c = 137.88 Å. A complete data set has been collected to 1.39 Å resolution. The asymmetric unit is estimated and confirmed by self-rotation function calculation to contain two molecules, giving a crystal volume per protein mass (VM) of 2.68 Å3 Da-1 and a solvent content of 54%. | |
650 | 7 | a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng |
700 | 1 | a Vevudova, Jitka4 aut |
700 | 1 | a Hatti-Kaul, Rajniu Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-rhk |
700 | 1 | a Su, Xiao-Dongu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)mbfys-xs |
710 | 2 | a Bioteknikb Centrum för tillämpade biovetenskaper4 org |
773 | 0 | t Acta Crystallographica. Section D: Biological Crystallographyg 59:3, s. 529-531q 59:3<529-531x 1399-0047 |
856 | 4 | u http://dx.doi.org/10.1107/S0907444902020747y FULLTEXT |
856 | 4 8 | u https://lup.lub.lu.se/record/129065 |
856 | 4 8 | u https://doi.org/10.1107/S0907444902020747 |
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