A novel strategy for the crystallization of proteins: X-ray diffraction validation.
Recently, the hypothesis was advanced that protein crystallization could be driven by the inclusion of small molecules rich in hydrogen-bonding, hydrophobic and electrostatic bonding possibilities. Conventional organic and biologically active molecules would promote lattice formation by their mediation of intermolecular interactions in crystals. The results of an extensive series of crystallization experiments strongly supported the idea. Here, difference Fourier X-ray diffraction analyses of nine crystals grown in the experiments are presented, which convincingly demonstrate the validity of the hypothesis and illustrate some of the ways in which small molecules can participate in lattice interactions.
Larson
Steven B
SB
Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697, USA.
Day
John S
JS
Cudney
Robert
R
McPherson
Alexander
A
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D005583:Fourier Analysis; D008024:Ligands; D008958:Models, Molecular; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry
D008024:Ligands; D011506:Proteins; D012259:Ribonuclease, Pancreatic; D009113:Muramidase; D014357:Trypsin