ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
Rhizomucor miehei aspartic proteinase (Mr = 38701, 361 residues) has been crystallized in a form suitable for analysis by X-ray diffraction. The flattened rod-shaped crystals were grown from polyethylene glycol 8000 using vapour-diffusion methods. The crystal form is in space group P212〈inf/〉121 [a = 41.67 (2), b = 51.21 (3) and c = 173.3 (2) Å], with Z = 4 and one molecule in the asymmetric unit. Data were collected over the range 0 〈 h 〈 14, 0 〈 k 〈 16 and 0 〈 l 〈 62, resulting in 7032 unique reflections to give 72.1% completeness with a merging R of 0.067 to a resolution limit of 2.8 Å. A molecular-replacement solution of the structure has been obtained using the aspartic proteinase from Rhizomucor pusillus as a model. Rigid-body refinement of the model and subsequent refinement using molecular dynamics were performed with X-PLOR, leading to a current R-factor of 20.1% for 2.8 Å data.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S090744499401156X
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