%0 Journal Article %1 ISI:A1996VW61600026 %A May, O %A Siemann, M %A Syldatk, C %A Niefind, K %A Schomburg, D %C 35 NORRE SOGADE, PO BOX 2148, DK-1016 COPENHAGEN, DENMARK %D 1996 %I MUNKSGAARD INT PUBL LTD %J ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY %K imported myown %N 6 %P 1209-1210 %R 10.1107/S0907444996007731 %T Crystallization and preliminary X-ray analysis of a hydantoinase from Arthrobacter aurescens DSM 3745 %U https://doi.org/10.1107/S0907444996007731 %V 52 %X L-Hydantoinase from Arthrobacter aurescens DSM 3745 has been purified to homogeneity and crystallized from polyethylene glycol solutions in a form suitable for X-ray diffraction analysis. The crystals have been grown by the sitting-drop variant of the vapour-diffusion method. X-ray diffraction studies show that the crystals belong to the monoclinic space group P2(1) with a = 111.2, b = 74.4, c = 146.5 Angstrom and beta = 106.7 degrees. Its asymmetric unit contains four monomers related by 222 symmetry. The crystals diffract to at least 2.6 Angstrom.

@article{ISI:A1996VW61600026, abstract = {{L-Hydantoinase from Arthrobacter aurescens DSM 3745 has been purified to homogeneity and crystallized from polyethylene glycol solutions in a form suitable for X-ray diffraction analysis. The crystals have been grown by the sitting-drop variant of the vapour-diffusion method. X-ray diffraction studies show that the crystals belong to the monoclinic space group P2(1) with a = 111.2, b = 74.4, c = 146.5 Angstrom and beta = 106.7 degrees. Its asymmetric unit contains four monomers related by 222 symmetry. The crystals diffract to at least 2.6 Angstrom.}}, added-at = {2018-01-25T13:38:08.000+0100}, address = {{35 NORRE SOGADE, PO BOX 2148, DK-1016 COPENHAGEN, DENMARK}}, affiliation = {{May, O (Reprint Author), UNIV STUTTGART,INST BIOVERFAHRENSTECH,ALLMANDRING 31,D-70569 STUTTGART,GERMANY. GBF,D-38124 BRAUNSCHWEIG,GERMANY.}}, author = {May, O and Siemann, M and Syldatk, C and Niefind, K and Schomburg, D}, biburl = {https://puma.ub.uni-stuttgart.de/bibtex/23499006463176e6d62cf9a890b4c26bf/siemannherzberg}, da = {{2018-01-25}}, doc-delivery-number = {{VW616}}, doi = {{10.1107/S0907444996007731}}, interhash = {26f9caa76c8e6f95e860c9a3f1871c6b}, intrahash = {3499006463176e6d62cf9a890b4c26bf}, issn = {{0907-4449}}, journal = {{ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}}, journal-iso = {{Acta Crystallogr. Sect. D-Biol. Crystallogr.}}, keywords = {imported myown}, keywords-plus = {{5-SUBSTITUTED HYDANTOINS; AMINO-ACIDS; MECHANISM}}, language = {{English}}, month = {{NOV 1}}, number = {{6}}, number-of-cited-references = {{17}}, oa = {{gold}}, orcid-numbers = {{Schomburg, Dietmar/0000-0002-3354-822X}}, pages = {{1209-1210}}, publisher = {{MUNKSGAARD INT PUBL LTD}}, research-areas = {{Biochemistry \& Molecular Biology; Biophysics; Crystallography}}, times-cited = {{8}}, timestamp = {2018-01-25T12:38:18.000+0100}, title = {{Crystallization and preliminary X-ray analysis of a hydantoinase from Arthrobacter aurescens DSM 3745}}, type = {{Article}}, unique-id = {{ISI:A1996VW61600026}}, url = {https://doi.org/10.1107/S0907444996007731}, usage-count-last-180-days = {{0}}, usage-count-since-2013 = {{1}}, volume = {{52}}, web-of-science-categories = {{Biochemical Research Methods; Biochemistry \& Molecular Biology; Biophysics; Crystallography}}, year = {{1996}} }