4EK7
High speed X-ray analysis of plant enzymes at room temperature
Summary for 4EK7
Entry DOI | 10.2210/pdb4ek7/pdb |
Descriptor | Raucaffricine-O-beta-D-glucosidase, beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | raucaffricine-o-beta-d-glucosidase, raucaffricine beta-glucosidase activity, hydrolase |
Biological source | Rauvolfia serpentina (devilpepper) |
Total number of polymer chains | 2 |
Total formula weight | 116093.92 |
Authors | Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. (deposition date: 2012-04-09, release date: 2013-02-20, Last modification date: 2023-11-08) |
Primary citation | Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. High speed X-ray analysis of plant enzymes at room temperature. Phytochemistry, 2012 Cited by PubMed Abstract: X-ray measurements at room temperature (295 K) deliver high quality data sets with unprecedented speed (<2 min), as shown for crystallized raucaffricine-O-β-D-glucosidase (RG), its mutant RG-Glu186Gln and several ligand complexes of the enzyme which participates in alkaloid biosynthesis in the plant Rauvolfia. The data obtained are compared with data sets measured under typical cryo conditions (100K). Under both conditions, density maps are highly comparable and favor the described protocol for room temperature measurements, potentially paving the way for future crystallographic studies capturing biosynthetic pathway intermediates. PubMed: 22704651DOI: 10.1016/j.phytochem.2012.05.009 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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