Control of substrate access to the active site in methane monooxygenase

Analysis of Substrate Access to Active Sites in Bacterial Multicomponent Monooxygenase Hydroxylases: X-ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase fromPseudomonassp. OX1

(2011) Michael S. McCormick et al.   BIOCHEMISTRY

XDS

(2010) Wolfgang Kabsch   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

PHENIX: a comprehensive Python-based system for macromolecular structure solution

(2010) Paul D. Adams et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Active Site Threonine Facilitates Proton Transfer during Dioxygen Activation at the Diiron Center of Toluene/o-Xylene Monooxygenase Hydroxylase

(2010) Woon Ju Song et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b

(2010) Nates An Elango et al.   PROTEIN SCIENCE

Revisiting the Mechanism of Dioxygen Activation in Soluble Methane Monooxygenase fromM. capsulatus(Bath): Evidence for a Multi-Step, Proton-Dependent Reaction Pathway

(2009) Christine E. Tinberg et al.   BIOCHEMISTRY

Structural consequences of effector protein complex formation in a diiron hydroxylase

(2008) L. J. Bailey et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA