2G51

anomalous substructure of trypsin (p1)

Summary for 2G51

• Entry DOI: 10.2210/pdb2g51/pdb
• Related: 2G4H 2G4I 2G4J 2G4K 2G4L 2G4M 2G4N 2G4O 2G4P 2G4Q 2G4R 2G4S 2G4T 2G4U 2G4V 2G4W 2G4X 2G4Y 2G4Z 2G52 2G55
• Descriptor: Trypsin, CHLORIDE ION (3 entities in total)
• Functional Keywords: anomalous substructure of trypsin (p1), hydrolase
• Biological source: Fusarium oxysporum
• Cellular location: Secreted: P35049
• Total number of polymer chains: 1
• Total formula weight: 22306.85

Authors

Mueller-Dieckmann, C.,Weiss, M.S. (deposition date: 2006-02-22, release date: 2007-02-20, Last modification date: 2024-10-30)

Primary citation

Mueller-Dieckmann, C.,Panjikar, S.,Schmidt, A.,Mueller, S.,Kuper, J.,Geerlof, A.,Wilmanns, M.,Singh, R.K.,Tucker, P.A.,Weiss, M.S.
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
Acta Crystallogr.,Sect.D, 63:366-380, 2007

PubMed Abstract: 23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.

PubMed: 17327674
DOI: 10.1107/S0907444906055624

Experimental method

X-RAY DIFFRACTION (1.84 Å)