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Hydration in Protein Crystals. A Neutron Diffraction Analysis of Carbonmonoxymyoglobin

Cheng X, Schoenborn BP
Acta Crystallogr., B 46 195-208 (1990)
Cited: 12 times

Reviews - 2mb5 mentioned but not cited (1)

  1. Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition. Liebschner D, Afonine PV, Moriarty NW, Langan P, Adams PD. Acta Crystallogr D Struct Biol 74 800-813 (2018)

Articles - 2mb5 mentioned but not cited (11)

  1. Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin. Ruscio JZ, Kumar D, Shukla M, Prisant MG, Murali TM, Onufriev AV. Proc. Natl. Acad. Sci. U.S.A. 105 9204-9209 (2008)
  2. An atomistic view on human hemoglobin carbon monoxide migration processes. Lucas MF, Guallar V. Biophys. J. 102 887-896 (2012)
  3. A computational study of water and CO migration sites and channels inside myoglobin. Lapelosa M, Abrams CF. J Chem Theory Comput 9 1265-1271 (2013)
  4. A strategy for reducing gross errors in the generalized Born models of implicit solvation. Onufriev AV, Sigalov G. J Chem Phys 134 164104 (2011)
  5. High-resolution crystal structures of protein helices reconciled with three-centered hydrogen bonds and multipole electrostatics. Kuster DJ, Liu C, Fang Z, Ponder JW, Marshall GR. PLoS ONE 10 e0123146 (2015)
  6. A novel energy-based stochastic method for positioning polar protons in protein structures from X-rays. Glick M, Goldblum A. Proteins 38 273-287 (2000)
  7. Full kinetics of CO entry, internal diffusion, and exit in myoglobin from transition-path theory simulations. Yu TQ, Lapelosa M, Vanden-Eijnden E, Abrams CF. J. Am. Chem. Soc. 137 3041-3050 (2015)
  8. Factors correlating with significant differences between X-ray structures of myoglobin. Rashin AA, Domagalski MJ, Zimmermann MT, Minor W, Chruszcz M, Jernigan RL. Acta Crystallogr. D Biol. Crystallogr. 70 481-491 (2014)
  9. Large-volume protein crystal growth for neutron macromolecular crystallography. Ng JD, Baird JK, Coates L, Garcia-Ruiz JM, Hodge TA, Huang S. Acta Crystallogr F Struct Biol Commun 71 358-370 (2015)
  10. X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): perdeuteration of proteins for neutron diffraction. Blum MM, Tomanicek SJ, John H, Hanson BL, Rüterjans H, Schoenborn BP, Langan P, Chen JC. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 379-385 (2010)
  11. Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin. Kovalevsky AY, Chatake T, Shibayama N, Park SY, Ishikawa T, Mustyakimov M, Fisher SZ, Langan P, Morimoto Y. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 270-273 (2008)




Related citations provided by authors (7)

  1. Real Space Refinement of Neutron Diffraction Data from Sperm Whale Carbonmonoxymyoglobin. Hanson JC, Schoenborn BP J. Mol. Biol. 153 117- (1981)
  2. The Determination of Structural Water by Neutron Protein Crystallography. An Analysis of the Carbon Monoxide Myoglobin Water Structure. Schoenborn BP, Hanson JC ACS Symp. Ser. 127 215- (1980)
  3. Neutron Diffraction Analysis and Real Space Refinement of met and Carbon Monoxide Myoglobin. Schoenborn BP, Norvell JC Acta Crystallogr A 31 32- (1975)
  4. Neutron Diffraction Analysis of Metmyoglobin. Schoenborn BP, Diamond R Brookhaven Symp. Biol. 27 3- (1975)
  5. Neutron Diffraction Analysis of Myoglobin. Structure of the Carbon Monoxide Derivative. Norvell JC, Nunes AC, Schoenborn BP Science 190 568- (1975)
  6. A Neutron Diffraction Analysis of Myoglobin. III. Hydrogen-Deuterium Bonding in Side Chains. Schoenborn BP Cold Spring Harb. Symp. Quant. Biol. 36 569- (1972)
  7. Neutron Diffraction Analysis of Myoglobin. Schoenborn BP Nature 224 143- (1969)

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